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FeMoco (FeMo cofactor) is the primary cofactor of nitrogenase. Nitrogenase is the enzyme that catalyzes the conversion of atmospheric nitrogen molecules N 2 into ammonia (NH 3 ) through the process known as nitrogen fixation .
The biosynthesis of the FeMoco active site is highly complex. [13] Structure of the FeMoco active site of nitrogenase. The molybdenum cofactor (pictured) is composed of a molybdenum-free organic complex called molybdopterin, which has bound an oxidized molybdenum(VI) atom through adjacent sulfur (or occasionally selenium) atoms. Except for the ...
Structure of the FeMoco cluster in nitrogenase. The cluster is linked to the protein by the amino acid residues cysteine and histidine. Nitrogenase include two P-clusters ([8Fe-7S]) and two FeMocos ([7Fe-9S-C-Mo-R homocitrate]). [8] Carbon monoxide dehydrogenase and acetyl coenzyme-A synthase each features an Fe-N-iS 4 clusters. [9] [10]
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The biosynthesis of the FeMoco active site is highly complex. [93] Structure of the FeMoco active site of nitrogenase The molybdenum cofactor (pictured) is composed of a molybdenum-free organic complex called molybdopterin, which has bound an oxidized molybdenum(VI) atom through adjacent sulfur (or occasionally selenium) atoms. Except for the ...
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1909 Ford Model T transmission with top of casing removed. Engine flywheel, with its integrated magneto, is on the left, the gear clutches are in the center, and the driveshaft is on the right side.
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