Redox Properties of Lysine- and Methionine-Coordinated Hemes Ensure Downhill Electron Transfer in NrfH(2)A(4) Nitrite Reductase

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Abstract

The multiheme NrfHA nitrite reductase is a menaquinol:nitrite oxidoreductase that catalyzes the 6-electron reduction of nitrite to ammonia in a reaction that involves eight protons. X-ray crystallography of the enzyme from Desulfovibrio vulgaris revealed that the biological unit, NrfH(2)A(4), houses 28 c-type heme groups, 22 of them with low spin and 6 with pentacoordinated high spin configuration. The high spin hemes, which are the electron entry and exit points of the complex, carry a highly unusual coordination for c-type hemes, lysine and methionine as proximal ligands in NrfA and NrfH, respectively. Employing redox titrations followed by X-band EPR spectroscopy and surface-enhanced resonance Raman spectroelectrochemistry, we provide the first experimental evidence for the midpoint redox potential of the NrfH menaquinol-interacting methionine-coordinated heme (-270 +/- 10 mV, z = 0.96), identified by the use of the inhibitor HQNO, a structural analogue of the physiological electron donor. The redox potential of the catalytic lysine-coordinated high spin heme of NrfA is -50 +/- 10 mV, z = 0.9. These values determined for the integral NrfH(2)A(4) complex indicate that a driving force for a downhill electron transfer is ensured in this complex.
Original languageUnknown
Pages (from-to)5637-5643
JournalJournal Of Physical Chemistry B
Volume116
Issue number19
DOIs
Publication statusPublished - 1 Jan 2012

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