2e80: Difference between revisions

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[[Image:2e80.jpg|left|200px]]
{{Seed}}
[[Image:2e80.png|left|200px]]


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{{STRUCTURE_2e80|  PDB=2e80  |  SCENE=  }}  
{{STRUCTURE_2e80|  PDB=2e80  |  SCENE=  }}  


'''Cytochrome c Nitrite Reductase from Wolinella succinogenes with bound substrate nitrite'''
===Cytochrome c Nitrite Reductase from Wolinella succinogenes with bound substrate nitrite===




==Overview==
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Cytochrome c nitrite reductase catalyzes the six-electron reduction of nitrite to ammonia without the release of potential reaction intermediates, such as NO or hydroxylamine. On the basis of the crystallographic observation of reaction intermediates and of density functional calculations, we present a working hypothesis for the reaction mechanism of this multiheme enzyme which carries a novel lysine-coordinated heme group (Fe-Lys). It is proposed that nitrite reduction starts with a heterolytic cleavage of the N-O bond which is facilitated by a pronounced back-bonding interaction of nitrite coordinated through nitrogen to the reduced (Fe(II)) but not the oxidized (Fe(III)) active site iron. This step leads to the formation of an [FeNO](6) species and a water molecule and is further facilitated by a hydrogen bonding network that induces an electronic asymmetry in the nitrite molecule that weakens one N-O bond and strengthens the other. Subsequently, two rapid one-electron reductions lead to an [FeNO](8) form and, by protonation, to an Fe(II)-HNO adduct. Hereafter, hydroxylamine will be formed by a consecutive two-electron two-proton step which is dehydrated in the final two-electron reduction step to give ammonia and an additional water molecule. A single electron reduction of the active site closes the catalytic cycle.
The line below this paragraph, {{ABSTRACT_PUBMED_12296741}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_12296741}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Mechanism of the six-electron reduction of nitrite to ammonia by cytochrome c nitrite reductase., Einsle O, Messerschmidt A, Huber R, Kroneck PM, Neese F, J Am Chem Soc. 2002 Oct 2;124(39):11737-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12296741 12296741]
Mechanism of the six-electron reduction of nitrite to ammonia by cytochrome c nitrite reductase., Einsle O, Messerschmidt A, Huber R, Kroneck PM, Neese F, J Am Chem Soc. 2002 Oct 2;124(39):11737-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12296741 12296741]
Structure of cytochrome c nitrite reductase., Einsle O, Messerschmidt A, Stach P, Bourenkov GP, Bartunik HD, Huber R, Kroneck PM, Nature. 1999 Jul 29;400(6743):476-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10440380 10440380]
Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 A resolution, inhibitor binding, and heme-packing motifs., Einsle O, Stach P, Messerschmidt A, Simon J, Kroger A, Huber R, Kroneck PM, J Biol Chem. 2000 Dec 15;275(50):39608-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10984487 10984487]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Wolinella succinogenes]]
[[Category: Wolinella succinogenes]]
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[[Category: Nitrite reductase]]
[[Category: Nitrite reductase]]
[[Category: Substrate complex]]
[[Category: Substrate complex]]
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