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Nitric Oxide Does Not Inhibit but Is Metabolized by the Cytochrome - Supercomplex. | LitMetric

Nitric Oxide Does Not Inhibit but Is Metabolized by the Cytochrome - Supercomplex.

Int J Mol Sci

Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory, 119991 Moscow, Russia.

Published: November 2020

AI Article Synopsis

Article Abstract

Nitric oxide (NO) is a well-known active site ligand and inhibitor of respiratory terminal oxidases. Here, we investigated the interaction of NO with a purified chimeric - supercomplex composed of cytochrome and -type terminal oxidase. Strikingly, we found that the enzyme in turnover with O and reductants is resistant to inhibition by the ligand, being able to metabolize NO at 25 °C with an apparent turnover number as high as ≈303 mol NO (mol enzyme) min at 30 µM NO. The rate of NO consumption proved to be proportional to that of O consumption, with 2.65 ± 0.19 molecules of NO being consumed per O molecule by the mycobacterial -. The enzyme was found to metabolize the ligand even under anaerobic reducing conditions with a turnover number of 2.8 ± 0.5 mol NO (mol enzyme) min at 25 °C and 8.4 µM NO. These results suggest a protective role of mycobacterial supercomplexes against NO stress.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7697965PMC
http://dx.doi.org/10.3390/ijms21228521DOI Listing

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