Flavocytochrome
From Proteopedia
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| - | <StructureSection load='1kbi' size=' | + | <StructureSection load='1kbi' size='450' side='right' scene='44/442751/Cv/2' caption='Yeast flavocytochrome b2 flavin-binding domain complex with FMN, MPD, phosphate, pyruvic acid (PDB code [[1kbi]]) '> |
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== Structural highlights == | == Structural highlights == | ||
<scene name='44/442751/Cv/3'>The biological assembly of Yeast flavocytochrome b2 flavin-binding domain is homotetramer</scene>. | <scene name='44/442751/Cv/3'>The biological assembly of Yeast flavocytochrome b2 flavin-binding domain is homotetramer</scene>. | ||
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| + | <scene name='44/442751/Cv/5'>Fe coordination site</scene>. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 12:25, 21 February 2016
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3D Structures of flavocytochrome
Updated on 21-February-2016
References
- ↑ Gondry M, Dubois J, Terrier M, Lederer F. The catalytic role of tyrosine 254 in flavocytochrome b2 (L-lactate dehydrogenase from baker's yeast). Comparison between the Y254F and Y254L mutant proteins. Eur J Biochem. 2001 Sep;268(18):4918-27. PMID:11559361
- ↑ Ost TW, Clark J, Mowat CG, Miles CS, Walkinshaw MD, Reid GA, Chapman SK, Daff S. Oxygen activation and electron transfer in flavocytochrome P450 BM3. J Am Chem Soc. 2003 Dec 10;125(49):15010-20. PMID:14653735 doi:http://dx.doi.org/10.1021/ja035731o
- ↑ Pankhurst KL, Mowat CG, Miles CS, Leys D, Walkinshaw MD, Reid GA, Chapman SK. Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina. Biochemistry. 2002 Jul 9;41(27):8551-6. PMID:12093271
