Sandbox Reserved 460

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'''Vitamin B12 Binding Protein'''
'''Vitamin B12 Binding Protein'''
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Nitrite reductase is an enzyme that belongs to the Oxidoreductase family for catalyzing the six-electron reduction of nitrite into ammonia, using the reduced ferredoxin as the electron donor. It is a monomeric protein with molecular mass near 66 kDa characterized by a unique active site which contains a single [4Fe-4S] cluster and a single siroheme (which serves as the binding site for nitrite) via a bridging sulfur atom from a cysteine residue. The protein has a globular fold consisting of 3 alpha/beta domains with the siroheme-iron sulfur cofactor at the interface of the three domains. The siroheme is surrounded by several ionizable amino acid residues that facilitate the binding and subsequent reduction of nitrite.
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Nitrite reductase is an enzyme that belongs to the Oxidoreductase family for catalyzing the six-electron reduction of nitrite into ammonia, using the reduced ferredoxin as the electron donor. It is a monomeric protein with molecular mass near 66 kDa characterized by a unique active site which contains a single <scene name='Sandbox_Reserved_460/Active_site/1'>[4Fe-4S] cluster</scene> and a single siroheme (which serves as the binding site for nitrite) via a bridging sulfur atom from a cysteine residue. The protein has a globular fold consisting of 3 alpha/beta domains with the siroheme-iron sulfur cofactor at the interface of the three domains. The siroheme is surrounded by several ionizable amino acid residues that facilitate the binding and subsequent reduction of nitrite.

Revision as of 21:19, 30 April 2012

Nitrite Reductase

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This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500.
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Vitamin B12 Binding Protein Nitrite reductase is an enzyme that belongs to the Oxidoreductase family for catalyzing the six-electron reduction of nitrite into ammonia, using the reduced ferredoxin as the electron donor. It is a monomeric protein with molecular mass near 66 kDa characterized by a unique active site which contains a single and a single siroheme (which serves as the binding site for nitrite) via a bridging sulfur atom from a cysteine residue. The protein has a globular fold consisting of 3 alpha/beta domains with the siroheme-iron sulfur cofactor at the interface of the three domains. The siroheme is surrounded by several ionizable amino acid residues that facilitate the binding and subsequent reduction of nitrite.

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