Electron paramagnetic resonance and magnetic circular dichroism studies of a hexa‐heme nitrite reductase from Wolinella succinogenes

FEBS Letters

Brittain, Thomas¹  Gadsby, Paul M.A.²  Greenwood, Colin²  Blackmore, Richard S.²  Thomson, Andrew J.² 

[1] Dept of Biochemistry, University of Auckland, Private Bag, Auckland, New Zealand;School of Biological Sciences and School of Chemical Sciences, University of East Anglia, Norwich NR4 7TJ, England

关键词: EPR;    MCD;    Heme-protein;    Nitrite reductase;    (Wolinella succinogenes);   

DOI  :  10.1016/0014-5793(87)81225-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The nature of the heme centers in the hexa-heme dissimilatory nitrite reductase from the bacterium Wolinella succinogenes has been investigated with EPR and magnetic circular dichroism spectroscopy. The EPR spectrum of the ferric enzyme is complex showing, in addition to magnetically isolated low-spin ferric hemes with g values of 2.93, 2.3 and 1.48, two sets of signals at g = 10.3, 3.7 and 4.8, 3.21, which we assign to two pairs of exchange coupled hemes. The MCD spectra show that the isolated hemes are bis-histidine coordinated and that there is one high-spin ferric heme. The exchange coupling is lost on treatment with SDS.

【 授权许可】

Unknown