Purification and characterization of NADPH-dependent Cr(VI) reductase from Escherichia coli ATCC 33456 SCIE SCOPUS KCI

Cited 68 time in WEB OF SCIENCE Cited 0 time in Scopus
Title
Purification and characterization of NADPH-dependent Cr(VI) reductase from Escherichia coli ATCC 33456
Author(s)
Bae, WC; Lee, HK; Choe, YC; Jahng, DJ; Lee, SH; Kim, SJ; Lee, JH; Jeong, BC
KIOST Author(s)
Lee, Jung Hyun(이정현)
Publication Year
2005-02
Abstract
A soluble Cr(VI) reductase was purified from the cytoplasm of Escherichia coli ATCC 33456. The molecular mass was estimated to be 84 and 42 kDa by gel filtration and SDS-polyacrylamide gel electrophoresis, respectively, indicating a dimeric structure. The pI was 4.66, and optimal enzyme activity was obtained at pH 6.5 and 37 degrees C. The most stable condition existed at pH 7.0. The purified enzyme used both NADPH and NADH as electron donors for Cr(VI) reduction, while NADPH was the better, conferring 61% higher activity than NADH. The K-m values for NADPH and NADH were determined to be 47.5 and 17.2 mu mol, and the V-max values 322 and 130.7 mu mol Cr(VI) min(-1)mg(-1) protein, respectively. The activity was strongly inhibited by N-ethylmalemide, Ag2+, Cd2+, Hg2+, and Zn2+. The antibody against the enzyme showed no immunological cross reaction with those of other Cr(VI) reducing strains.
ISSN
1225-8873
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/5103
Bibliographic Citation
JOURNAL OF MICROBIOLOGY, v.43, no.1, pp.21 - 27, 2005
Publisher
MICROBIOLOGICAL SOCIETY KOREA
Subject
PSEUDOMONAS-AMBIGUA G-1; HEXAVALENT CHROMIUM; ENTEROBACTER-CLOACAE; ENZYMATIC REDUCTION; CHROMATE REDUCTASE; MEMBRANE; PROTEINS; CULTURES; PUTIDA; STRAIN
Keywords
Cr(VI) reductase; Escherichia coli ATCC 33456; purification
Type
Article
Language
English
Document Type
Article
Publisher
MICROBIOLOGICAL SOCIETY KOREA
Related Researcher
Research Interests

marine biotechnology,molecular microbiology,해양생명공학,분자미생물학

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