Thermodynamic Analysis of Denaturant-Induced Unfolding of HodC69S Protein Supports a Three-State Mechanism-Reference-Cited by-同舟云学术

Thermodynamic Analysis of Denaturant-Induced Unfolding of HodC69S Protein Supports a Three-State Mechanism

Published:2008-06-13 Issue:27 Volume:47 Page:7116-7126
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Boehm Kristian¹,Guddorf Jessica¹,Albers Alexander¹,Kamiyama Tadashi¹,Fetzner Susanne¹,Hinz H.-J.¹

Affiliation:

1. Institut für Physikalische Chemie, Westfälische Wilhelms-Universität Münster, Corrensstrasse 30, 48149 Münster, Germany, Institut für Molekulare Mikrobiologie and Biotechnologie, Westfälische Wilhelms-Universität Münster, Corrensstrasse 3, 48149 Münster, Germany, and Department of Chemistry, Kinki University, 3-4-1 Kowakae, Higashi-Osaka, Osaka, Japan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi800554v

Reference51 articles.

1. Bacterial 2,4-Dioxygenases: New Members of the α/β Hydrolase-Fold Superfamily of Enzymes Functionally Related to Serine Hydrolases

2. Oxygenases without requirement for cofactors or metal ions

3. Stability, Unfolding, and Structural Changes of Cofactor-Free 1H-3-Hydroxy-4-oxoquinaldine 2,4-Dioxygenase

4. Dioxygenases without Requirement for Cofactors and Their Chemical Model Reaction: Compulsory Order Ternary Complex Mechanism of 1H-3-Hydroxy-4-oxoquinaldine 2,4-Dioxygenase Involving General Base Catalysis by Histidine 251 and Single-Electron Oxidation of the Substrate Dianion

5. Thermodynamics of Denaturant-Induced Unfolding of a Protein That Exhibits Variable Two-State Denaturation

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