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Reconstruction of HydSL Hydrogenase from Thiocapsa roseopersicina after Cyanide Inhibition

Authors
  • Zorin, N. A.1
  • Khusnutdinova, A. N.1
  • Starodubov, A. S.1
  • Proskuryakov, I. I.1
  • Tsygankov, A. A.1
  • 1 Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290, Russia , Pushchino (Russia)
Type
Published Article
Journal
Applied Biochemistry and Microbiology
Publisher
Pleiades Publishing
Publication Date
May 01, 2021
Volume
57
Issue
3
Pages
351–355
Identifiers
DOI: 10.1134/S0003683821030169
Source
Springer Nature
Keywords
License
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Abstract

AbstractIt is shown that the catalytic center of Thiocapsa roseopersicina remains active after prolonged treatment with cyanide. It was found that the incubation of cyanide-treated hydrogenase in the presence of beta-mercaptoethanol, ferric iron, and sodium sulfide restored the hydrogenase activity in the hydrogen-oxidation reaction in the presence of methylviologen. The process of activity reconstruction depended on time and reached its maximum value (~ 60%) within 30 min at room temperature. In this case, an absorption band at 420 nm appeared in the absorption spectrum of the hydrogenase, which was present in the native hydrogenase and disappeared after treatment with cyanide; this indicated the reconstruction of iron–sulfur clusters. Thus, instead of growing bacteria in the presence of an iron isotope, one can replace 56Fe with 57Fe in the isolated enzyme, which will allow the use of smaller amounts of 57Fe.

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