The formate complex of the cytochrome bo quinol oxidase of Escherichia coli exhibits a ‘g = 12’ EPR feature analogous to that of ‘slow’ cytochrome oxidase

FEBS Letters

Calhoun, Melissa W.²  Gennis, Robert B.²  Salerno, John C.¹ 

[1] Biology Department and Center for Biochemistry and Biophysics, Rensselaer Polytechnic Institute, Troy, NY 12180, USA;School of Chemical Sciences, University of Illinois at Urbana Champaign, Urbana, IL 61801, USA

关键词: Quinol oxidase;    Cytochrome bo;    Formate complex;    EPR;    E. coli;    TES;    N-tris[hydroxymethyl]methyl-2-aminoethanesulfonic acid;    EDTA;    ethylenediamine tetraacetic acid;    EPR;    electron paramagnetic resonance;   

DOI  :  10.1016/0014-5793(92)81079-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The cytochrome bo quinol oxidase of Escherichia coli is homologous in sequence and in structure to cytochrome aa ₃ type cytochrome oxidase in subunit 1, which contains the catalytic core. The cytochrome bo enzyme forms a formate complex which exhibits ‘g = 12’ and ‘g = 2.9’ EPR signals at X band; similar signals have previously been observed only in association with the ‘slow’ and formate-ligated states of cytochrome oxidase. These signals arise from transitions within integral spin multiplets identified with the homologous heme-copper binuclear catalytic centers in both enzymes.

【 授权许可】

Unknown