Regulating the nitrite reductase activity of myoglobin by redesigning the heme active center
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- 作者：Lei-Bin Wua ; 1 ; Hong Yuanb ; 1 ; Shu-Qin Gaoc ; Yong Youc ; Chang-Ming Niea ; Ge-Bo Wenc ; Ying-Wu Lina ; c ; linlinying@hotmail.com" class="auth_mail" title="E-mail the corresponding author ; ywlin@usc.edu.cn" class="auth_mail" title="E-mail the corresponding author ; Xiangshi Tanb ; xstan@fudan.edu.cn" class="auth_mail" title="E-mail the corresponding author
- 关键词：Heme proteins ; Protein design ; Nitrite reductase ; EPR ; X-ray crystallography
- 刊名：Nitric Oxide
- 出版年：2016
- 出版时间：1 July 2016
- 年：2016
- 卷：57
- 期：Complete
- 页码：21-29
- 全文大小：1953 K
文摘
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The nitrite reductase activity of myoglobin was regulated by redesign of its heme center.
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A single distal histidine with a suitable position to the heme iron is crucial for nitrite reduction.
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Creation of a channel to the heme center significantly enhanced the nitrite reductase activity.
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X-ray crystal structures revealed unique substrate and product binding models in the heme center.
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This study enriched the structure and nitrite reductase activity relationship of heme proteins.