scholarly journals MvhB-type polyferredoxin as an electron-transfer chain in putative redox-enzyme complexes

2020 ◽  
Author(s):  
Tomohiro Watanabe ◽  
Seigo Shima
1992 ◽  
Vol 25 (3) ◽  
pp. 253-324 ◽  
Author(s):  
John E. Walker

The inner membranes of mitochondria contain three multi-subunit enzyme complexes that act successively to transfer electrons from NADH to oxygen, which is reduced to water (Fig. I). The first enzyme in the electron transfer chain, NADH:ubiquinone oxidoreductase (or complex I), is the subject of this review. It removes electrons from NADH and passes them via a series of enzyme-bound redox centres (FMN and Fe-S clusters) to the electron acceptor ubiquinone. For each pair of electrons transferred from NADH to ubiquinone it is usually considered that four protons are removed from the matrix (see section 4.1 for further discussion of this point).


2009 ◽  
Vol 75 (12) ◽  
pp. 4202-4205 ◽  
Author(s):  
Wei Wang ◽  
Feng-Qing Wang ◽  
Dong-Zhi Wei

ABSTRACT A new cytochrome P450 monooxygenase, FcpC, from Streptomyces virginiae IBL-14 has been identified. This enzyme is found to be responsible for the bioconversion of a pyrano-spiro steroid (diosgenone) to a rare nuatigenin-type spiro steroid (isonuatigenone), which is a novel C-25-hydroxylated diosgenone derivative. A whole-cell P450 system was developed for the production of isonuatigenone via the expression of the complete three-component electron transfer chain in an Escherichia coli strain.


Author(s):  
M. Fátima C. Guedes da Silva ◽  
Cristina M. P. Ferreira ◽  
João J. R. Fraústo da Silva ◽  
Armando J. L. Pombeiro

2021 ◽  
pp. 3-38
Author(s):  
Jian-Ren Shen ◽  
Yoshiki Nakajima ◽  
Fusamichi Akita ◽  
Michihiro Suga

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