2024-03-29T04:34:51Z
https://nagoya.repo.nii.ac.jp/oai
oai:nagoya.repo.nii.ac.jp:00005109
2023-01-16T03:49:41Z
643:666:667
Disulfide-bond formation in the H+-pyrophosphatase of Streptomyces coelicolor and its implications for redox control and enzyme structure
Mimura, Hisatoshi
Nakanishi, Yoichi
Maeshima, Masayoshi
前島, 正義
open access
H+-PPase
Redox control
Proton pump
Streptomyces coelicolor
Redox control of disulfide-bond formation in the H+-pyrophosphatase of Streptomyces coelicolor was investigated using cysteine mutants expressed in Escherichia coli. The wildtype enzyme, but not a cysteine-less mutant, was reversibly inactivated by oxidation. To determine the residues involved in oxidative inactivation, different cysteine residues were replaced. Analysis with a cysteine-modifying reagent revealed that the formation of a disulfide bond between cysteines 253 and 621 was responsible for enzyme inactivation. This result suggests that residues in different cytoplasmic loops are close to each other in the tertiary structure. Both cysteine residues are conserved in K+-independent (type II) H+- pyrophosphatases.
Elsevier
2005-07
eng
journal article
VoR
http://hdl.handle.net/2237/6662
https://nagoya.repo.nii.ac.jp/records/5109
FEBS Letters
579
17
3625
3631
https://nagoya.repo.nii.ac.jp/record/5109/files/2005-FEBS_Lett-ScPP.pdf
application/pdf
691.9 kB
2018-02-19