Stabilization of cytochrome b₅ by a conserved tyrosine in the secondary sphere of heme active site: A spectroscopic and computational study

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• 作者：Shan Hu^a ; Bo He^a ; Xiao-Juan Wang^a ; Shu-Qin Gao^b ; Ge-Bo Wen^b ; Ying-Wu Lin^a ; ^b ; ^{linlinying@hotmail.com} ; ^{ywlin@usc.edu.cn}
• 关键词：Heme proteins ; Cyt b5 ; Secondary sphere ; Unfolding ; Heme transfer
• 刊名：Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
• 出版年：2017
• 出版时间：5 March 2017
• 年：2017
• 卷：174
• 期：Complete
• 页码：118-123
• 全文大小：1030 K
• 卷排序：174

文摘

The stabilization role of a conserved Tyr30 in Cyt b5 was studied. Both Y30F Cyt b5 and Y30H Cyt b5 mutants exhibit reduced thermal stability. Rate constant of heme transfer to apo-Mb: Y30H Cyt b5 > Y30F Cyt b5 > WT Cyt b5. Both hydrophobic and H-bonding interactions of Tyr30 contribute to protein stability. This study provides clues for design of artificial heme proteins.