Regulation of both the structure and function by a de novo designed disulfide bond: a case study of heme proteins in myoglobin. Issue 34 (12th April 2018)

• Record Type: Journal Article
• Authors: Yin, Lu-Lu; Yuan, Hong; Du, Ke-Jie; He, Bo; Gao, Shu-Qin; Wen, Ge-Bo; Tan, Xiangshi; Lin, Ying-Wu
• Is Part Of: Chemical communications. Volume 54:Issue 34(2018)
• Page Start: 4356
• Page End: 4359
• Publication Date: 2018-04-12
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c8cc01646a
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : The V21C/V66C/F46S myoglobin mutant, with a de novo designed intramolecular disulfide bond resembling that in cytoglobin without structural evidence, exhibits a dehalogenation activity exceeding that of a native dehaloperoxidase. Abstract : A de novo designed intramolecular disulfide bond in myoglobin, resembling that in cytoglobin without structural evidence, was confirmed by an X-ray structure for the first time and was demonstrated to regulate both the structure and function of this protein, which fulfills the design of an artificial dehaloperoxidase, with an activity exceeding that of a native enzyme.