Insights into the mode of flavin mononucleotide binding and catalytic mechanism of bacterial chromate reductases: A molecular dynamics simulation study-Reference-Cited by-同舟云学术

Insights into the mode of flavin mononucleotide binding and catalytic mechanism of bacterial chromate reductases: A molecular dynamics simulation study

Published:2019-05-26 Issue:10 Volume:120 Page:16990-17005
ISSN:0730-2312
Container-title:Journal of Cellular Biochemistry
language:en
Short-container-title:J Cell Biochem

Author:

Pradhan Sukanta Kumar¹²,Singh Nihar Ranjan³,Dehury Budheswar⁴⁵,Panda Debashis⁶,Modi Mahendra Kumar⁶,Thatoi Hrudayanath⁷

Affiliation:

1. Department of Bioinformatics Odisha University of Agriculture and Technology Bhubaneswar Odisha India

2. Department of Biotechnology, School of Life Sciences Ravenshaw University Cuttack Odisha India

3. Department of Botany, School of Life Sciences Ravenshaw University Cuttack Odisha India

4. Biomedical Informatics Centre Regional Medical Research Centre (ICMR) Nalco Square, Chandrasekharpur Bhubaneswar Odisha India

5. Department of Chemistry Technical University of Denmark DK‐2800 Kgs Lyngby

6. Department of Agricultural Biotechnology Assam Agricultural University Jorhat Assam India

7. Department of Biotechnology North Orissa University Sriram Chandra Vihar, Takatpur Baripada Odisha India

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/jcb.28960

Reference34 articles.

1. Bacterial chromate reductase, a potential enzyme for bioremediation of hexavalent chromium: A review

2. Characterization of enzymatic reduction of hexavalent chromium by Escherichia coli ATCC 33456

3. Investigation on mechanism of Cr(VI) reduction and removal by Bacillus amyloliquefaciens, a novel chromate tolerant bacterium isolated from chromite mine soil

4. Hexavalent Chromium Reduction by Free and Immobilized Cell-free Extract of Arthrobacter rhombi-RE

5. Analysis of Novel Soluble Chromate and Uranyl Reductases and Generation of an Improved Enzyme by Directed Evolution

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