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Surface cysteines could protect the SARS-CoV-2 main protease from oxidative damage.
Ravanfar, Raheleh; Sheng, Yuling; Shahgholi, Mona; Lomenick, Brett; Jones, Jeff; Chou, Tsui-Fen; Gray, Harry B; Winkler, Jay R.
  • Ravanfar R; Beckman Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA.
  • Sheng Y; Beckman Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA.
  • Shahgholi M; Beckman Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA.
  • Lomenick B; Beckman Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA.
  • Jones J; Beckman Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA.
  • Chou TF; Beckman Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA.
  • Gray HB; Beckman Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA. Electronic address: hbgray@caltech.edu.
  • Winkler JR; Beckman Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA. Electronic address: winklerj@caltech.edu.
J Inorg Biochem ; 234: 111886, 2022 09.
Article in English | MEDLINE | ID: covidwho-1930970
ABSTRACT
The SARS-CoV-2 main protease (Mpro) is responsible for cleaving twelve nonstructural proteins from the viral polyprotein. Mpro, a cysteine protease, is characterized by a large number of noncatalytic cysteine (Cys) residues, none involved in disulfide bonds. In the absence of a tertiary-structure stabilizing role for these residues, a possible alternative is that they are involved in redox processes. We report experimental work in support of a proposal that surface cysteines on Mpro can protect the active-site Cys145 from oxidation by reactive oxygen species (ROS). In investigations of enzyme kinetics, we found that mutating three surface cysteines to serines did not greatly affect activity, which in turn indicates that these cysteines could protect Cys145 from oxidative damage.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Oxidative Stress / Cysteine / Coronavirus 3C Proteases / SARS-CoV-2 Language: English Journal: J Inorg Biochem Year: 2022 Document Type: Article Affiliation country: J.jinorgbio.2022.111886

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Oxidative Stress / Cysteine / Coronavirus 3C Proteases / SARS-CoV-2 Language: English Journal: J Inorg Biochem Year: 2022 Document Type: Article Affiliation country: J.jinorgbio.2022.111886