Flavocytochrome: Difference between revisions

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<StructureSection load='1kbi' size='350' side='right' scene='44/442751/Cv/2' caption='Yeast flavocytochrome b2 flavin-binding domain dimer complex with FMN, MPD, phosphate, pyruvic acid (PDB code [[1kbi]]) '>
<StructureSection load='2b7r' size='450' side='right' caption='Structure of heme-containing flavocytochrome c3 complex with FAD and fumaric acid (PDB code [[2b7r]]).' scene='' >




* '''Flavocytochrome b2''' (Fcb2) is a flavin-dependent hydroxy acid dehydrogenase<ref>PMID:11559361</ref> 
* '''Flavocytochrome c''' or '''flavocytochrome c sulphide dehydrogenase''' or '''Fcc''' catalyzes the conversion of H2S and ferricytochrome c to S and ferrocytochrome c.<br />
.<br />
*  '''FP450 BM3''' is a fatty acid hydroxtylase from ''Bacillus'' ''megaterium''<ref>PMID:14653735</ref> 
.<br />
* '''Fcc''' catalyzes the conversion of H2S and ferricytochrome c to S and ferrocytochrome c.<br />
*  '''Fcc3''' has fumarate reductase activity<ref>PMID:12093271</ref>   
*  '''Fcc3''' has fumarate reductase activity<ref>PMID:12093271</ref>   
.
* '''Flavocytochrome b2''' is a L-lactate/cytochrome c oxidoreductase<ref>PMID:15260495</ref>  
</StructureSection>
* '''Flavocytochrome b558''' is the catalytic component of the phagocyte NADPH oxidase


== 3D Structures of flavocytochrome ==
<scene name='44/442751/Cv/10'>Structure of heme-containing flavocytochrome c3 complex with FAD and fumaric acid</scene> (PDB code [[2b7r]]<ref>PMID:16699170</ref>).
*<scene name='44/442751/Cv/12'>1st Heme binding site</scene>. Water molecules are shown as red spheres.
*<scene name='44/442751/Cv/13'>1st Heme Fe coordination site</scene>.
*<scene name='44/442751/Cv/14'>2nd Heme binding site</scene>.
*<scene name='44/442751/Cv/15'>2nd Heme Fe coordination site</scene>.
*<scene name='44/442751/Cv/16'>3rd Heme binding site</scene>.
*<scene name='44/442751/Cv/17'>3rd Heme Fe coordination site</scene>.
*<scene name='44/442751/Cv/18'>4th Heme binding site</scene>.
*<scene name='44/442751/Cv/19'>4th Heme Fe coordination site</scene>.


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Interestedly, that all 4 heme groups are <scene name='44/442751/Cv/20'>covalently bound with Cys residues</scene> in heme-containing flavocytochrome c3 (PDB code [[2b7r]]).
{{#tree:id=OrganizedByTopic|openlevels=0|


*FP450
<scene name='44/442751/Cv/26'>All Fe of 4 heme groups are coordinated with His residues</scene>.


**[[3kx3]], [[3kx4]], [[3kx5]], [[3ekb]], [[3ekd]], [[3ekf]], [[3nnb]], [[2yqo]], [[2yqp]], [[1p0v]], [[1p0w]], [[1p0x]], [[1jme]] – BmFP450 BM3 (mutant) – ''Bacillus megaterium''<br />
<scene name='44/442751/Cv/22'>Fumaric acid binding site</scene>.
**[[2ij2]] - BmFP450 BM3<br />
**[[2uwh]] - BmFP450 BM3 (mutant)+palmitic acid<br />
**[[2j1m]], [[2j4s]] - BmFP450 BM3 + DMSO<br />
**[[3ben]] - BmFP450 BM3 heme domain+inhibitor<br />
**[[3vrd]] – Fc heme and FMN binding domains – ''Thermochromatium tepidum''


*Fcb2
<scene name='44/442751/Cv/24'>FAD binding site</scene>.


**[[3ks0]] – mFcb2 heme domain+fragment antigen binding B2B4+Cyt b2 – mouse<br />
<scene name='44/442751/Cv/25'>Na coordination site</scene>.
**[[2oz0]], [[1qcw]] – yFcb2 (mutant) – yeast<br />
**[[1kbi]], [[1fcb]] – yFcb2<br />
**[[1kbj]] – yFcb2 FMN binding domain<br />
**[[1sze]] – yFcb2 (mutant)+benzoylformate<br />
**[[1szf]], [[1lco]], [[1ldc]] – yFcb2 (mutant)+pyruvate derivative<br />
**[[1szg]] – yFcb2 (mutant)+sulfite<br />
**[[1ltd]] – yFcb2 +sulfite


*Fcc
== 3D Structures of flavocytochrome ==
[[Flavocytochrome 3D structures]]


**[[2b7r]], [[2b7s]], [[1q9i]], [[1p2e]], [[1p2h]], [[1lj1]], [[1m64]], [[1kss]], [[1ksu]], [[1jrx]], [[1jry]], [[1jrz]], [[1e39]] – SfFcc3 (mutant) – ''Shewanella frigidimarina''<br />
</StructureSection>
**[[1qo8]], [[1qjd]] - SfFcc3<br />
**[[1y0p]] – SfFcc3+mesaconate<br />
**[[1wve]] – Fcc+4-cresol dehydrogenase – ''Pseudomonas putida''
 
*Fc B558


**[[1wlp]] – Fc B558 - human
}}
== References ==
== References ==
<references/>
<references/>


[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 09:17, 25 June 2024


  • Flavocytochrome c or flavocytochrome c sulphide dehydrogenase or Fcc catalyzes the conversion of H2S and ferricytochrome c to S and ferrocytochrome c.
  • Fcc3 has fumarate reductase activity[1]
  • Flavocytochrome b2 is a L-lactate/cytochrome c oxidoreductase[2]
  • Flavocytochrome b558 is the catalytic component of the phagocyte NADPH oxidase

(PDB code 2b7r[3]).

  • . Water molecules are shown as red spheres.
  • .
  • .
  • .
  • .
  • .
  • .
  • .

Interestedly, that all 4 heme groups are in heme-containing flavocytochrome c3 (PDB code 2b7r).

.

.

.

.

3D Structures of flavocytochrome

Flavocytochrome 3D structures


Structure of heme-containing flavocytochrome c3 complex with FAD and fumaric acid (PDB code 2b7r).

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ 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
  2. ↑ Mowat CG, Wehenkel A, Green AJ, Walkinshaw MD, Reid GA, Chapman SK. Altered substrate specificity in flavocytochrome b2: structural insights into the mechanism of L-lactate dehydrogenation. Biochemistry. 2004 Jul 27;43(29):9519-26. PMID:15260495 doi:http://dx.doi.org/10.1021/bi049263m
  3. ↑ Pankhurst KL, Mowat CG, Rothery EL, Hudson JM, Jones AK, Miles CS, Walkinshaw MD, Armstrong FA, Reid GA, Chapman SK. A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina. J Biol Chem. 2006 Jul 21;281(29):20589-97. Epub 2006 May 12. PMID:16699170 doi:http://dx.doi.org/10.1074/jbc.M603077200

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Michal Harel, Alexander Berchansky, Joel L. Sussman
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