Metal specificity of the Ni(ii) and Zn(ii) binding sites of the N-terminal and G-domain of E. coli HypB-Reference-Cited by-同舟云学术

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Metal specificity of the Ni(ii) and Zn(ii) binding sites of the N-terminal and G-domain of E. coli HypB

Published:2021 Issue:36 Volume:50 Page:12635-12647
ISSN:1477-9226
Container-title:Dalton Transactions
language:en
Short-container-title:Dalton Trans.

Author:

Hecel Aleksandra¹^ORCID,Kola Arian²,Valensin Daniela²,Kozlowski Henryk¹³,Rowinska-Zyrek Magdalena¹^ORCID

Affiliation:

1. Faculty of Chemistry, University of Wroclaw, F. Joliot-Curie 14, 50-383 Wroclaw, Poland

2. Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via A. Moro 2, 53100 Siena, Italy

3. Institute of Health Sciences, University of Opole, 68 Katowicka St., 45-060 Opole, Poland

Abstract

HypB is one of the chaperones required for proper nickel insertion into [NiFe]-hydrogenase.

Funder

Narodowe Centrum Nauki

Narodowa Agencja Wymiany Akademickiej

Publisher

Royal Society of Chemistry (RSC)

Subject

Inorganic Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2021/DT/D1DT02126E

Reference50 articles.

1. Metal ions in biological catalysis: from enzyme databases to general principles

2. Metalloproteins and metal sensing

3. Microbial metalloproteomes are largely uncharacterized

4. Nutrient metal elements in plants

5. Identification and preliminary characterization of AcsF, a putative Ni-insertase used in the biosynthesis of acetyl-CoA synthase from Clostridium thermoaceticum

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1. –HH and –HAAAH motifs act as fishing nets for biologically relevant metal ions in metallopeptides;Journal of Inorganic Biochemistry;2024-03

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