KOPRI Repository

Biochemical and structural basis of mercuric reductase, GbsMerA, from Gelidibacter salicanalis PAMC21136

Cited 0 time in wos
Cited 0 time in scopus

Full metadata record

DC Field Value Language
dc.contributor.author이민주-
dc.contributor.authorBashu Dev Pardhe-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorDo, Hackwon-
dc.contributor.author오태진-
dc.date.accessioned2023-12-06T16:39:07Z-
dc.date.available2023-12-06T16:39:07Z-
dc.date.issued2023-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/14950-
dc.description.abstractHeavy metals, including mercury, are non-biodegradable and highly toxic to microorganisms even at low concentrations. Understanding the mechanisms underlying the environmental adaptability of microorganisms with Hg resistance holds promise for their use in Hg bioremediation. We characterized GbsMerA, a mercury reductase belonging to the mercury-resistant operon of Gelidibacter salicanalis PAMC21136, and found its maximum activity of 474.7 μmole/min/mg in reducing Hg+2. In the presence of Ag and Mn, the enzyme exhibited moderate activity as 236.5 μmole/min/mg and 69 μmole/min/mg, respectively. GbsMerA exhibited optimal activity at pH 7.0 and a temperature of 60 °C. Moreover, the crystal structure of GbsMerA and structural comparison with homologues indicated that GbsMerA contains residues, Tyr437´ and Asp47, which may be responsible for metal transfer at the si-face by providing a hydroxyl group (-OH) to abstract a proton from the thiol group of cysteine. The complex structure with NADPH indicated that Y174 in the re-face can change its side chain direction upon NADPH binding, indicating that Y174 may have a role as a gate for NADPH binding. Moreover, the heterologous host expressing GbsMerA (pGbsMerA) is more resistant to Hg toxicity when compared to the host lacking GbsMerA. Overall, this study provides a background for understanding the catalytic mechanism and Hg detoxification by GbsMerA and suggests the application of genetically engineered E. coli strains for environmental Hg removal.-
dc.languageEnglish-
dc.subject.classification해당사항없음-
dc.titleBiochemical and structural basis of mercuric reductase, GbsMerA, from Gelidibacter salicanalis PAMC21136-
dc.title.alternative극지 미생물 Gelidibacter salicanalis PAMC21136로부터 유래한 수은 환원효소 GbsMerA의 생화학적 및 구조적 기초 연구-
dc.typeArticle-
dc.identifier.bibliographicCitation이민주, et al. 2023. "Biochemical and structural basis of mercuric reductase, GbsMerA, from Gelidibacter salicanalis PAMC21136". <em>SCIENTIFIC REPORTS</em>, 13(17854): 1-11.-
dc.citation.titleSCIENTIFIC REPORTS-
dc.citation.volume13-
dc.citation.number17854-
dc.identifier.doi10.1038/s41598-023-44968-w-
dc.citation.startPage1-
dc.citation.endPage11-
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2021:25.676-
dc.subject.keywordHeavy metal detoxification?-
dc.subject.keywordHg resistance-
dc.subject.keywordMercuric reductase-
dc.identifier.localId2023-0216-
Appears in Collections  
2023-2023, Development of potential antibiotic compounds using polar organism resources (23-23) / Lee, Jun Hyuck (PM23030)
Files in This Item
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse