Author Correction: A cytochrome c is the natural electron acceptor for nicotine oxidoreductase
نویسندگان
چکیده
A Correction to this paper has been published: https://doi.org/10.1038/s41589-021-00756-z.
منابع مشابه
Cytochrome electron spin resonance line shapes, ligand fields, and components stoichiometry in ubiquinol-cytochrome c oxidoreductase.
The EPR spectra of the cytochromes in ubiquinol-cytochrome c oxidoreductase (Complex III) have peaks at g = 3.78 (cytochrome b566) g = 3.45 (cytochrome b562) and g = 3.35 (cytochrome c1). The highly asymmetric peak of cytochrome b566 has been simulated using an arbitrary gaussian distribution of crystal field parameters. The asymmetry is due to the nonlinear relationship between field position ...
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Selenate reductase (SER) from Thauera selenatis is a periplasmic enzyme that has been classified as a type II molybdoenzyme. The enzyme comprises three subunits SerABC, where SerC is an unusual b-heme cytochrome. In the present work the spectropotentiometric characterization of the SerC component and the identification of redox partners to SER are reported. The mid-point redox potential of the ...
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N,N'-dicyclohexylcarbodiimide (DCCD) has been reported to inhibit steady-state proton translocation by cytochrome bc(1) and b(6)f complexes without significantly altering the rate of electron transport, a process referred to as decoupling. In chromatophores of the purple bacterium Rhodobacter sphaeroides, this has been associated with the specific labeling of a surface-exposed aspartate-187 of ...
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The isolation and partial characterization of a flavoprotein which functions as the electron acceptor of trimethylamine dehydrogenase (EC 1.5.99.7) from a methylotrophic bacterium is described. It has a molecular weight of 77,000 and is composed of two dissimilar subunits. All preparations examined contained only 1 mol of FAD/m01 of the flavoprotein. Trimethylamine dehydrogenase, in the presenc...
متن کاملMembrane-bound cytochrome c is an alternative electron donor for cytochrome aa3 in Nitrobacter winogradskyi.
We purified membrane-bound cytochrome c-550 [cytochrome c-550(m)] to an electrophoretically homogeneous state from Nitrobacter winogradskyi. The cytochrome showed peaks at 409 and 525 nm in the oxidized form and peaks at 416, 521, and 550 nm in the reduced form. The molecular weight of the cytochrome was estimated to be 18,400 on the basis of protein and heme c contents and 18,600 by gel filtra...
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ژورنال
عنوان ژورنال: Nature Chemical Biology
سال: 2021
ISSN: ['1552-4450', '1552-4469']
DOI: https://doi.org/10.1038/s41589-021-00756-z