Detailed Active Site Configuration of a New Crystal Form of Methanol Dehydrogenase from Methylophilus W3A1 at 1.9 Å Resolution,-Reference-Cited by-同舟云学术

Detailed Active Site Configuration of a New Crystal Form of Methanol Dehydrogenase from Methylophilus W3A1 at 1.9 Å Resolution,

Published:1998-12-31 Issue:4 Volume:38 Page:1214-1220
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Xia Zong-xiang¹,He Yong-ning¹,Dai Wei-wen¹,White Scott A.¹,Boyd Geoffrey D.¹,Mathews F. Scott¹

Affiliation:

1. Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China, and Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9822574

Reference31 articles.

1. The structure and function of methanol dehydrogenase and related quinoproteins containing pyrrolo-quinoline quinone

2. Salisbury, S. A., Forrest, H. S., Cruse, W. B. T., andKennard, O. (1979)Nature280, 843−844.

3. Characterization of mutant forms of the quinoprotein methanol dehydrogenase lacking an essential calcium ion

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