期刊
PROTEIN SCIENCE
卷 26, 期 2, 页码 218-226出版社
WILEY-BLACKWELL
DOI: 10.1002/pro.3071
关键词
azurin; circular permutation; reduction potential; secondary coordination sphere
资金
- US National Science Foundation [CHE14-13328]
- US National Institute of Health [NIH R01GM054803]
- National Science Foundation of China [31500641, 81302687]
- Tianjin Municipal Science and Technology Commission [14JCYBJC43400, 13ZCZDSY04800, 14ZCZDSY00059]
- Chinese Society of Biotechnology
- National Science Foundation [DGE-0925180]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1413328] Funding Source: National Science Foundation
Type 1 copper (T1Cu) proteins are electron transfer (ET) proteins involved in many important biological processes. While the effects of changing primary and secondary coordination spheres in the T1Cu ET function have been extensively studied, few report has explored the effect of the overall protein structural perturbation on active site configuration or reduction potential of the protein, even though the protein scaffold has been proposed to play a critical role in enforcing the entatic or rack-induced state for ET functions. We herein report circular permutation of azurin by linking the N- and C-termini and creating new termini in the loops between 1(st) and 2(nd) strands or between 3(rd) and 4(th) strands. Characterization by electronic absorption, electron paramagnetic spectroscopies, as well as crystallography and cyclic voltammetry revealed that, while the overall structure and the primary coordination sphere of the circular permutated azurins remain the same as those of native azurin, their reduction potentials increased by 18 and 124 mV over that of WTAz. Such increases in reduction potentials can be attributed to subtle differences in the hydrogen-bonding network in secondary coordination sphere around the T1Cu center. PDB Code(s):
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