derivative profiling omics package (dpop) Search Results


dpo4  (Verlag GmbH)
90
Verlag GmbH dpo4
Dpo4, supplied by Verlag GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/derivative+profiling+omics+package+(dpop)/taq+polymerase/10__1002_slash_cbic__201300296-53-26-2
Average 90 stars, based on 1 article reviews
dpo4 - by Bioz Stars, 2026-09
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dpol_t4  (InterPro Inc)
90
InterPro Inc dpol_t4
Dpol T4, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/derivative+profiling+omics+package+(dpop)/dpol+t4/pmc06008273__13568_2018_630_MOESM1_ESM-1140-3-1
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dpol_t4 - by Bioz Stars, 2026-09
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grassroots dpos  (INGOS Ltd)
90
INGOS Ltd grassroots dpos
Interviews held in <t> Burkina </t> Faso.
Grassroots Dpos, supplied by INGOS Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/derivative+profiling+omics+package+(dpop)/grassroots+dpos/pmc06489163-30-18-28
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grassroots dpos - by Bioz Stars, 2026-09
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dpor bch nb  (Neuroscience Information Framework)
86
Neuroscience Information Framework dpor bch nb
a , A schematic overview illustrating structures from key nitrogenase and Nfl proteins with their associated metalloclusters responsible for electron transfer and catalysis. Electrons are sequentially transferred through transient interaction of the homodimeric reductase components to the metal cofactors of the heterotetrameric catalytic components. All reductase components harbour an [Fe S ]-cluster, which donates electrons to the subunit bridging metallocofactor of the catalytic component. For the <t>DPOR</t> (Bch(NB) 2 ) and FeMoco maturase Nif(EN) 2 , this is an [Fe S ]-cluster , , while the Mo-nitrogenase catalytic component (Nif(DK) 2 ) harbours a P-cluster ([Fe 8 S 7 ]-cluster) as an electron relay to the active site . In DPOR, the substrate protochlorophyllide a (Pchlide) sits directly at the active site , . Nitrogenases harbour more complex metalloclusters in their active sites, such as FeMoco , and Nif(EN) 2 harbours the [Fe 8 S 9 C]-cluster . The metallocluster composition for the methylthio-alkane reductase as well as the stoichiometry of the reaction was still unresolved. The protein name of each subunit is shown and derived from the corresponding gene name. Genes for each nitrogenase(-like) enzyme are usually organized in an individual operon encoding the subunits of reductase and catalytic components. Not shown here is the very distant homologue Ni 2+ -sirohydrochlorin a , c -diamide reductase (CfbD), which catalyses the second last step of coenzyme F 430 biosynthesis, a tetrapyrrole cofactor in methanogens . b , Main catalytic reactions. DPOR reduces the C17=C18 double bond of Pchlide to chlorophyllide a (Chlide) in the chlorophyll a biosynthetic pathway , . The Nif(EN) 2 maturase converts the precursor [Fe 8 S 9 C]-cluster into FeMoco by inserting Mo and ( R )-homocitrate . Mo-nitrogenase reduces protons and N 2 to NH 3 and H 2 (ref. ). The methylthio-alkane reductase is proposed to reduce MT-EtOH to methanethiol and C 2 H (ref. ). Protein phylogenetic relationships are depicted based on Extended Data Fig. . c , Legend of the metalloclusters found in nitrogenase and Nfl proteins shown in a .
Dpor Bch Nb, supplied by Neuroscience Information Framework, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/derivative+profiling+omics+package+(dpop)/bch+dpor+nb/pmc12552129-28-2-9
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dpor bch nb - by Bioz Stars, 2026-09
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digital phosphor oscilloscope (dpos) tektronix tds3000b-series  (Tektronix inc)
90
Tektronix inc digital phosphor oscilloscope (dpos) tektronix tds3000b-series
a , A schematic overview illustrating structures from key nitrogenase and Nfl proteins with their associated metalloclusters responsible for electron transfer and catalysis. Electrons are sequentially transferred through transient interaction of the homodimeric reductase components to the metal cofactors of the heterotetrameric catalytic components. All reductase components harbour an [Fe S ]-cluster, which donates electrons to the subunit bridging metallocofactor of the catalytic component. For the <t>DPOR</t> (Bch(NB) 2 ) and FeMoco maturase Nif(EN) 2 , this is an [Fe S ]-cluster , , while the Mo-nitrogenase catalytic component (Nif(DK) 2 ) harbours a P-cluster ([Fe 8 S 7 ]-cluster) as an electron relay to the active site . In DPOR, the substrate protochlorophyllide a (Pchlide) sits directly at the active site , . Nitrogenases harbour more complex metalloclusters in their active sites, such as FeMoco , and Nif(EN) 2 harbours the [Fe 8 S 9 C]-cluster . The metallocluster composition for the methylthio-alkane reductase as well as the stoichiometry of the reaction was still unresolved. The protein name of each subunit is shown and derived from the corresponding gene name. Genes for each nitrogenase(-like) enzyme are usually organized in an individual operon encoding the subunits of reductase and catalytic components. Not shown here is the very distant homologue Ni 2+ -sirohydrochlorin a , c -diamide reductase (CfbD), which catalyses the second last step of coenzyme F 430 biosynthesis, a tetrapyrrole cofactor in methanogens . b , Main catalytic reactions. DPOR reduces the C17=C18 double bond of Pchlide to chlorophyllide a (Chlide) in the chlorophyll a biosynthetic pathway , . The Nif(EN) 2 maturase converts the precursor [Fe 8 S 9 C]-cluster into FeMoco by inserting Mo and ( R )-homocitrate . Mo-nitrogenase reduces protons and N 2 to NH 3 and H 2 (ref. ). The methylthio-alkane reductase is proposed to reduce MT-EtOH to methanethiol and C 2 H (ref. ). Protein phylogenetic relationships are depicted based on Extended Data Fig. . c , Legend of the metalloclusters found in nitrogenase and Nfl proteins shown in a .
Digital Phosphor Oscilloscope (Dpos) Tektronix Tds3000b Series, supplied by Tektronix inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/derivative+profiling+omics+package+(dpop)/digital+oscilloscope/us06980212-109-3-2
Average 90 stars, based on 1 article reviews
digital phosphor oscilloscope (dpos) tektronix tds3000b-series - by Bioz Stars, 2026-09
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dpo chemical  (Oxchem Corporation)
90
Oxchem Corporation dpo chemical
a , A schematic overview illustrating structures from key nitrogenase and Nfl proteins with their associated metalloclusters responsible for electron transfer and catalysis. Electrons are sequentially transferred through transient interaction of the homodimeric reductase components to the metal cofactors of the heterotetrameric catalytic components. All reductase components harbour an [Fe S ]-cluster, which donates electrons to the subunit bridging metallocofactor of the catalytic component. For the <t>DPOR</t> (Bch(NB) 2 ) and FeMoco maturase Nif(EN) 2 , this is an [Fe S ]-cluster , , while the Mo-nitrogenase catalytic component (Nif(DK) 2 ) harbours a P-cluster ([Fe 8 S 7 ]-cluster) as an electron relay to the active site . In DPOR, the substrate protochlorophyllide a (Pchlide) sits directly at the active site , . Nitrogenases harbour more complex metalloclusters in their active sites, such as FeMoco , and Nif(EN) 2 harbours the [Fe 8 S 9 C]-cluster . The metallocluster composition for the methylthio-alkane reductase as well as the stoichiometry of the reaction was still unresolved. The protein name of each subunit is shown and derived from the corresponding gene name. Genes for each nitrogenase(-like) enzyme are usually organized in an individual operon encoding the subunits of reductase and catalytic components. Not shown here is the very distant homologue Ni 2+ -sirohydrochlorin a , c -diamide reductase (CfbD), which catalyses the second last step of coenzyme F 430 biosynthesis, a tetrapyrrole cofactor in methanogens . b , Main catalytic reactions. DPOR reduces the C17=C18 double bond of Pchlide to chlorophyllide a (Chlide) in the chlorophyll a biosynthetic pathway , . The Nif(EN) 2 maturase converts the precursor [Fe 8 S 9 C]-cluster into FeMoco by inserting Mo and ( R )-homocitrate . Mo-nitrogenase reduces protons and N 2 to NH 3 and H 2 (ref. ). The methylthio-alkane reductase is proposed to reduce MT-EtOH to methanethiol and C 2 H (ref. ). Protein phylogenetic relationships are depicted based on Extended Data Fig. . c , Legend of the metalloclusters found in nitrogenase and Nfl proteins shown in a .
Dpo Chemical, supplied by Oxchem Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/derivative+profiling+omics+package+(dpop)/dpo+chemical/pmc05391282-300-0-5
Average 90 stars, based on 1 article reviews
dpo chemical - by Bioz Stars, 2026-09
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sulfolobus solfataricus dpo4  (Kunkel GmbH)
90
Kunkel GmbH sulfolobus solfataricus dpo4
a , A schematic overview illustrating structures from key nitrogenase and Nfl proteins with their associated metalloclusters responsible for electron transfer and catalysis. Electrons are sequentially transferred through transient interaction of the homodimeric reductase components to the metal cofactors of the heterotetrameric catalytic components. All reductase components harbour an [Fe S ]-cluster, which donates electrons to the subunit bridging metallocofactor of the catalytic component. For the <t>DPOR</t> (Bch(NB) 2 ) and FeMoco maturase Nif(EN) 2 , this is an [Fe S ]-cluster , , while the Mo-nitrogenase catalytic component (Nif(DK) 2 ) harbours a P-cluster ([Fe 8 S 7 ]-cluster) as an electron relay to the active site . In DPOR, the substrate protochlorophyllide a (Pchlide) sits directly at the active site , . Nitrogenases harbour more complex metalloclusters in their active sites, such as FeMoco , and Nif(EN) 2 harbours the [Fe 8 S 9 C]-cluster . The metallocluster composition for the methylthio-alkane reductase as well as the stoichiometry of the reaction was still unresolved. The protein name of each subunit is shown and derived from the corresponding gene name. Genes for each nitrogenase(-like) enzyme are usually organized in an individual operon encoding the subunits of reductase and catalytic components. Not shown here is the very distant homologue Ni 2+ -sirohydrochlorin a , c -diamide reductase (CfbD), which catalyses the second last step of coenzyme F 430 biosynthesis, a tetrapyrrole cofactor in methanogens . b , Main catalytic reactions. DPOR reduces the C17=C18 double bond of Pchlide to chlorophyllide a (Chlide) in the chlorophyll a biosynthetic pathway , . The Nif(EN) 2 maturase converts the precursor [Fe 8 S 9 C]-cluster into FeMoco by inserting Mo and ( R )-homocitrate . Mo-nitrogenase reduces protons and N 2 to NH 3 and H 2 (ref. ). The methylthio-alkane reductase is proposed to reduce MT-EtOH to methanethiol and C 2 H (ref. ). Protein phylogenetic relationships are depicted based on Extended Data Fig. . c , Legend of the metalloclusters found in nitrogenase and Nfl proteins shown in a .
Sulfolobus Solfataricus Dpo4, supplied by Kunkel GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/derivative+profiling+omics+package+(dpop)/sulfolobus+solfataricus+dpo4/pm29487211-389-22-4
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calculated ir spectra of the derivatives of dpo  (Verlag GmbH)
90
Verlag GmbH calculated ir spectra of the derivatives of dpo
a , A schematic overview illustrating structures from key nitrogenase and Nfl proteins with their associated metalloclusters responsible for electron transfer and catalysis. Electrons are sequentially transferred through transient interaction of the homodimeric reductase components to the metal cofactors of the heterotetrameric catalytic components. All reductase components harbour an [Fe S ]-cluster, which donates electrons to the subunit bridging metallocofactor of the catalytic component. For the <t>DPOR</t> (Bch(NB) 2 ) and FeMoco maturase Nif(EN) 2 , this is an [Fe S ]-cluster , , while the Mo-nitrogenase catalytic component (Nif(DK) 2 ) harbours a P-cluster ([Fe 8 S 7 ]-cluster) as an electron relay to the active site . In DPOR, the substrate protochlorophyllide a (Pchlide) sits directly at the active site , . Nitrogenases harbour more complex metalloclusters in their active sites, such as FeMoco , and Nif(EN) 2 harbours the [Fe 8 S 9 C]-cluster . The metallocluster composition for the methylthio-alkane reductase as well as the stoichiometry of the reaction was still unresolved. The protein name of each subunit is shown and derived from the corresponding gene name. Genes for each nitrogenase(-like) enzyme are usually organized in an individual operon encoding the subunits of reductase and catalytic components. Not shown here is the very distant homologue Ni 2+ -sirohydrochlorin a , c -diamide reductase (CfbD), which catalyses the second last step of coenzyme F 430 biosynthesis, a tetrapyrrole cofactor in methanogens . b , Main catalytic reactions. DPOR reduces the C17=C18 double bond of Pchlide to chlorophyllide a (Chlide) in the chlorophyll a biosynthetic pathway , . The Nif(EN) 2 maturase converts the precursor [Fe 8 S 9 C]-cluster into FeMoco by inserting Mo and ( R )-homocitrate . Mo-nitrogenase reduces protons and N 2 to NH 3 and H 2 (ref. ). The methylthio-alkane reductase is proposed to reduce MT-EtOH to methanethiol and C 2 H (ref. ). Protein phylogenetic relationships are depicted based on Extended Data Fig. . c , Legend of the metalloclusters found in nitrogenase and Nfl proteins shown in a .
Calculated Ir Spectra Of The Derivatives Of Dpo, supplied by Verlag GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/derivative+profiling+omics+package+(dpop)/calculated+ir+spectra+of+the+derivatives+of+dpo/10__1002_slash_cjoc__201090262-34-14-35
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calculated ir spectra of the derivatives of dpo - by Bioz Stars, 2026-09
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dpo4 target gene  (Synbio Technologies LLC)
90
Synbio Technologies LLC dpo4 target gene
a , A schematic overview illustrating structures from key nitrogenase and Nfl proteins with their associated metalloclusters responsible for electron transfer and catalysis. Electrons are sequentially transferred through transient interaction of the homodimeric reductase components to the metal cofactors of the heterotetrameric catalytic components. All reductase components harbour an [Fe S ]-cluster, which donates electrons to the subunit bridging metallocofactor of the catalytic component. For the <t>DPOR</t> (Bch(NB) 2 ) and FeMoco maturase Nif(EN) 2 , this is an [Fe S ]-cluster , , while the Mo-nitrogenase catalytic component (Nif(DK) 2 ) harbours a P-cluster ([Fe 8 S 7 ]-cluster) as an electron relay to the active site . In DPOR, the substrate protochlorophyllide a (Pchlide) sits directly at the active site , . Nitrogenases harbour more complex metalloclusters in their active sites, such as FeMoco , and Nif(EN) 2 harbours the [Fe 8 S 9 C]-cluster . The metallocluster composition for the methylthio-alkane reductase as well as the stoichiometry of the reaction was still unresolved. The protein name of each subunit is shown and derived from the corresponding gene name. Genes for each nitrogenase(-like) enzyme are usually organized in an individual operon encoding the subunits of reductase and catalytic components. Not shown here is the very distant homologue Ni 2+ -sirohydrochlorin a , c -diamide reductase (CfbD), which catalyses the second last step of coenzyme F 430 biosynthesis, a tetrapyrrole cofactor in methanogens . b , Main catalytic reactions. DPOR reduces the C17=C18 double bond of Pchlide to chlorophyllide a (Chlide) in the chlorophyll a biosynthetic pathway , . The Nif(EN) 2 maturase converts the precursor [Fe 8 S 9 C]-cluster into FeMoco by inserting Mo and ( R )-homocitrate . Mo-nitrogenase reduces protons and N 2 to NH 3 and H 2 (ref. ). The methylthio-alkane reductase is proposed to reduce MT-EtOH to methanethiol and C 2 H (ref. ). Protein phylogenetic relationships are depicted based on Extended Data Fig. . c , Legend of the metalloclusters found in nitrogenase and Nfl proteins shown in a .
Dpo4 Target Gene, supplied by Synbio Technologies LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/derivative+profiling+omics+package+(dpop)/dpo4+target+gene/us10704031-25-1-15
Average 90 stars, based on 1 article reviews
dpo4 target gene - by Bioz Stars, 2026-09
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tektronix dpo 70000x  (Tektronix inc)
90
Tektronix inc tektronix dpo 70000x
a , A schematic overview illustrating structures from key nitrogenase and Nfl proteins with their associated metalloclusters responsible for electron transfer and catalysis. Electrons are sequentially transferred through transient interaction of the homodimeric reductase components to the metal cofactors of the heterotetrameric catalytic components. All reductase components harbour an [Fe S ]-cluster, which donates electrons to the subunit bridging metallocofactor of the catalytic component. For the <t>DPOR</t> (Bch(NB) 2 ) and FeMoco maturase Nif(EN) 2 , this is an [Fe S ]-cluster , , while the Mo-nitrogenase catalytic component (Nif(DK) 2 ) harbours a P-cluster ([Fe 8 S 7 ]-cluster) as an electron relay to the active site . In DPOR, the substrate protochlorophyllide a (Pchlide) sits directly at the active site , . Nitrogenases harbour more complex metalloclusters in their active sites, such as FeMoco , and Nif(EN) 2 harbours the [Fe 8 S 9 C]-cluster . The metallocluster composition for the methylthio-alkane reductase as well as the stoichiometry of the reaction was still unresolved. The protein name of each subunit is shown and derived from the corresponding gene name. Genes for each nitrogenase(-like) enzyme are usually organized in an individual operon encoding the subunits of reductase and catalytic components. Not shown here is the very distant homologue Ni 2+ -sirohydrochlorin a , c -diamide reductase (CfbD), which catalyses the second last step of coenzyme F 430 biosynthesis, a tetrapyrrole cofactor in methanogens . b , Main catalytic reactions. DPOR reduces the C17=C18 double bond of Pchlide to chlorophyllide a (Chlide) in the chlorophyll a biosynthetic pathway , . The Nif(EN) 2 maturase converts the precursor [Fe 8 S 9 C]-cluster into FeMoco by inserting Mo and ( R )-homocitrate . Mo-nitrogenase reduces protons and N 2 to NH 3 and H 2 (ref. ). The methylthio-alkane reductase is proposed to reduce MT-EtOH to methanethiol and C 2 H (ref. ). Protein phylogenetic relationships are depicted based on Extended Data Fig. . c , Legend of the metalloclusters found in nitrogenase and Nfl proteins shown in a .
Tektronix Dpo 70000x, supplied by Tektronix inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/derivative+profiling+omics+package+(dpop)/digital+and+mixed+signal+oscilloscopes+mso+dpo70000+series/us11050505-39-27-26
Average 90 stars, based on 1 article reviews
tektronix dpo 70000x - by Bioz Stars, 2026-09
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dpoc 4088 (or dp 4088  (Diakron Pharmaceuticals)
90
Diakron Pharmaceuticals dpoc 4088 (or dp 4088
a , A schematic overview illustrating structures from key nitrogenase and Nfl proteins with their associated metalloclusters responsible for electron transfer and catalysis. Electrons are sequentially transferred through transient interaction of the homodimeric reductase components to the metal cofactors of the heterotetrameric catalytic components. All reductase components harbour an [Fe S ]-cluster, which donates electrons to the subunit bridging metallocofactor of the catalytic component. For the <t>DPOR</t> (Bch(NB) 2 ) and FeMoco maturase Nif(EN) 2 , this is an [Fe S ]-cluster , , while the Mo-nitrogenase catalytic component (Nif(DK) 2 ) harbours a P-cluster ([Fe 8 S 7 ]-cluster) as an electron relay to the active site . In DPOR, the substrate protochlorophyllide a (Pchlide) sits directly at the active site , . Nitrogenases harbour more complex metalloclusters in their active sites, such as FeMoco , and Nif(EN) 2 harbours the [Fe 8 S 9 C]-cluster . The metallocluster composition for the methylthio-alkane reductase as well as the stoichiometry of the reaction was still unresolved. The protein name of each subunit is shown and derived from the corresponding gene name. Genes for each nitrogenase(-like) enzyme are usually organized in an individual operon encoding the subunits of reductase and catalytic components. Not shown here is the very distant homologue Ni 2+ -sirohydrochlorin a , c -diamide reductase (CfbD), which catalyses the second last step of coenzyme F 430 biosynthesis, a tetrapyrrole cofactor in methanogens . b , Main catalytic reactions. DPOR reduces the C17=C18 double bond of Pchlide to chlorophyllide a (Chlide) in the chlorophyll a biosynthetic pathway , . The Nif(EN) 2 maturase converts the precursor [Fe 8 S 9 C]-cluster into FeMoco by inserting Mo and ( R )-homocitrate . Mo-nitrogenase reduces protons and N 2 to NH 3 and H 2 (ref. ). The methylthio-alkane reductase is proposed to reduce MT-EtOH to methanethiol and C 2 H (ref. ). Protein phylogenetic relationships are depicted based on Extended Data Fig. . c , Legend of the metalloclusters found in nitrogenase and Nfl proteins shown in a .
Dpoc 4088 (Or Dp 4088, supplied by Diakron Pharmaceuticals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/derivative+profiling+omics+package+(dpop)/investigational+oral+anticoagulant+drug+dpoc+4088++or+dp+4088+/pmc05488177-259-28-5
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dpoc 4088 (or dp 4088 - by Bioz Stars, 2026-09
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fluorescent dpoc/chol liposomes  (FormuMax Inc)
90
FormuMax Inc fluorescent dpoc/chol liposomes
a , A schematic overview illustrating structures from key nitrogenase and Nfl proteins with their associated metalloclusters responsible for electron transfer and catalysis. Electrons are sequentially transferred through transient interaction of the homodimeric reductase components to the metal cofactors of the heterotetrameric catalytic components. All reductase components harbour an [Fe S ]-cluster, which donates electrons to the subunit bridging metallocofactor of the catalytic component. For the <t>DPOR</t> (Bch(NB) 2 ) and FeMoco maturase Nif(EN) 2 , this is an [Fe S ]-cluster , , while the Mo-nitrogenase catalytic component (Nif(DK) 2 ) harbours a P-cluster ([Fe 8 S 7 ]-cluster) as an electron relay to the active site . In DPOR, the substrate protochlorophyllide a (Pchlide) sits directly at the active site , . Nitrogenases harbour more complex metalloclusters in their active sites, such as FeMoco , and Nif(EN) 2 harbours the [Fe 8 S 9 C]-cluster . The metallocluster composition for the methylthio-alkane reductase as well as the stoichiometry of the reaction was still unresolved. The protein name of each subunit is shown and derived from the corresponding gene name. Genes for each nitrogenase(-like) enzyme are usually organized in an individual operon encoding the subunits of reductase and catalytic components. Not shown here is the very distant homologue Ni 2+ -sirohydrochlorin a , c -diamide reductase (CfbD), which catalyses the second last step of coenzyme F 430 biosynthesis, a tetrapyrrole cofactor in methanogens . b , Main catalytic reactions. DPOR reduces the C17=C18 double bond of Pchlide to chlorophyllide a (Chlide) in the chlorophyll a biosynthetic pathway , . The Nif(EN) 2 maturase converts the precursor [Fe 8 S 9 C]-cluster into FeMoco by inserting Mo and ( R )-homocitrate . Mo-nitrogenase reduces protons and N 2 to NH 3 and H 2 (ref. ). The methylthio-alkane reductase is proposed to reduce MT-EtOH to methanethiol and C 2 H (ref. ). Protein phylogenetic relationships are depicted based on Extended Data Fig. . c , Legend of the metalloclusters found in nitrogenase and Nfl proteins shown in a .
Fluorescent Dpoc/Chol Liposomes, supplied by FormuMax Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/derivative+profiling+omics+package+(dpop)/dir+labeled+liposomes/bio_rxiv__214908-156-0-6
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Image Search Results


Interviews held in Burkina Faso.

Journal: African Journal of Disability

Article Title: Disabled people’s organisations and the disability movement: Perspectives from Burkina Faso

doi: 10.4102/ajod.v8i0.500

Figure Lengend Snippet: Interviews held in Burkina Faso.

Article Snippet: Rather than a disability ‘movement’ in the western sense, in Burkina Faso, there is a multitude of grassroots DPOs, some of whom are supported by international non-governmental organisations (INGOs).

Techniques:

a , A schematic overview illustrating structures from key nitrogenase and Nfl proteins with their associated metalloclusters responsible for electron transfer and catalysis. Electrons are sequentially transferred through transient interaction of the homodimeric reductase components to the metal cofactors of the heterotetrameric catalytic components. All reductase components harbour an [Fe S ]-cluster, which donates electrons to the subunit bridging metallocofactor of the catalytic component. For the DPOR (Bch(NB) 2 ) and FeMoco maturase Nif(EN) 2 , this is an [Fe S ]-cluster , , while the Mo-nitrogenase catalytic component (Nif(DK) 2 ) harbours a P-cluster ([Fe 8 S 7 ]-cluster) as an electron relay to the active site . In DPOR, the substrate protochlorophyllide a (Pchlide) sits directly at the active site , . Nitrogenases harbour more complex metalloclusters in their active sites, such as FeMoco , and Nif(EN) 2 harbours the [Fe 8 S 9 C]-cluster . The metallocluster composition for the methylthio-alkane reductase as well as the stoichiometry of the reaction was still unresolved. The protein name of each subunit is shown and derived from the corresponding gene name. Genes for each nitrogenase(-like) enzyme are usually organized in an individual operon encoding the subunits of reductase and catalytic components. Not shown here is the very distant homologue Ni 2+ -sirohydrochlorin a , c -diamide reductase (CfbD), which catalyses the second last step of coenzyme F 430 biosynthesis, a tetrapyrrole cofactor in methanogens . b , Main catalytic reactions. DPOR reduces the C17=C18 double bond of Pchlide to chlorophyllide a (Chlide) in the chlorophyll a biosynthetic pathway , . The Nif(EN) 2 maturase converts the precursor [Fe 8 S 9 C]-cluster into FeMoco by inserting Mo and ( R )-homocitrate . Mo-nitrogenase reduces protons and N 2 to NH 3 and H 2 (ref. ). The methylthio-alkane reductase is proposed to reduce MT-EtOH to methanethiol and C 2 H (ref. ). Protein phylogenetic relationships are depicted based on Extended Data Fig. . c , Legend of the metalloclusters found in nitrogenase and Nfl proteins shown in a .

Journal: Nature Catalysis

Article Title: Methylthio-alkane reductases use nitrogenase metalloclusters for carbon–sulfur bond cleavage

doi: 10.1038/s41929-025-01426-2

Figure Lengend Snippet: a , A schematic overview illustrating structures from key nitrogenase and Nfl proteins with their associated metalloclusters responsible for electron transfer and catalysis. Electrons are sequentially transferred through transient interaction of the homodimeric reductase components to the metal cofactors of the heterotetrameric catalytic components. All reductase components harbour an [Fe S ]-cluster, which donates electrons to the subunit bridging metallocofactor of the catalytic component. For the DPOR (Bch(NB) 2 ) and FeMoco maturase Nif(EN) 2 , this is an [Fe S ]-cluster , , while the Mo-nitrogenase catalytic component (Nif(DK) 2 ) harbours a P-cluster ([Fe 8 S 7 ]-cluster) as an electron relay to the active site . In DPOR, the substrate protochlorophyllide a (Pchlide) sits directly at the active site , . Nitrogenases harbour more complex metalloclusters in their active sites, such as FeMoco , and Nif(EN) 2 harbours the [Fe 8 S 9 C]-cluster . The metallocluster composition for the methylthio-alkane reductase as well as the stoichiometry of the reaction was still unresolved. The protein name of each subunit is shown and derived from the corresponding gene name. Genes for each nitrogenase(-like) enzyme are usually organized in an individual operon encoding the subunits of reductase and catalytic components. Not shown here is the very distant homologue Ni 2+ -sirohydrochlorin a , c -diamide reductase (CfbD), which catalyses the second last step of coenzyme F 430 biosynthesis, a tetrapyrrole cofactor in methanogens . b , Main catalytic reactions. DPOR reduces the C17=C18 double bond of Pchlide to chlorophyllide a (Chlide) in the chlorophyll a biosynthetic pathway , . The Nif(EN) 2 maturase converts the precursor [Fe 8 S 9 C]-cluster into FeMoco by inserting Mo and ( R )-homocitrate . Mo-nitrogenase reduces protons and N 2 to NH 3 and H 2 (ref. ). The methylthio-alkane reductase is proposed to reduce MT-EtOH to methanethiol and C 2 H (ref. ). Protein phylogenetic relationships are depicted based on Extended Data Fig. . c , Legend of the metalloclusters found in nitrogenase and Nfl proteins shown in a .

Article Snippet: For the DPOR (Bch(NB) 2 ) and FeMoco maturase Nif(EN) 2 , this is an [Fe S ]-cluster , , while the Mo-nitrogenase catalytic component (Nif(DK) 2 ) harbours a P-cluster ([Fe 8 S 7 ]-cluster) as an electron relay to the active site .

Techniques: Derivative Assay