Redox potential of the cytochrome c in the flavocytochrome p‐cresol methylhydroxylase

FEBS Letters

Hopper, David J.¹ 

[1] Department of Biochemistry, University College of Wales, Aberystwyth, Dyfed SY23 3DD, Wales Great Britain

关键词: p-Cresol methylhydroxylase;    Flavocytochrome;    Cytochrome c;    Redox potential;    Reconstitution;   

DOI  :  10.1016/0014-5793(83)80738-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The redox potential of the cytochrome c in 5 flavocytochrome c proteins, all p-cresol methylhydroxylases purified from species of Pseudomonas, was measured. All gave similar values ranging from 226–250 mV. Two of the enzymes, from Pseudomonas putida NC1B 9866 and NC1B 9869, were resolved into their flavoprotein and cytochrome subunits and the redox potentials of the isolated cytochrome c subunits measured. The values for these were 60–70 mV below those for the whole enzymes but, in both cases, reconstitution of active enzyme by addition of the flavoprotein subunit restored the original potential.

【 授权许可】

Unknown