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dpor bch nb  (Neuroscience Information Framework)
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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
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bet dpor tnml 132 111 s [mz/gl]  (Chemie GmbH)
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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 .
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Image Search Results


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