期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 134, 期 19, 页码 8241-8253出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja302190r
关键词
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资金
- ANPCyT [PICT 2007-0314]
- CONICET
- Alexander von Humboldt
- K.S. Krishnan Research Associateship fellowships
- Max-Planck-Society
- NIH [DK019038]
- Stanford GCEP
- [SFB 624]
Bioinorganic canon states that active-site thiolate coordination promotes rapid electron transfer (ET) to and from type 1 copper proteins. In recent work, we have found that copper ET sites in proteins also can be constructed without thiolate ligation (called type zero sites). Here we report multifrequency electron paramagnetic resonance (EPR), magnetic circular dichroism (MCD), and nuclear magnetic resonance (NMR) spectroscopic data together with density functional theory (DFT) and spectroscopy-oriented configuration interaction (SORCI) calculations for type zero Pseudomonas aeruginosa azurin variants. Wild-type (type 1) and type zero copper centers experience virtually identical ligand fields. Moreover, O-donor covalency is enhanced in type zero centers relative that in the C112D (type 2) protein. At the same time, N-donor covalency is reduced in a similar fashion to type 1 centers. QM/MM and SORCI calculations show that the electronic structures of type zero and type 2 are intimately linked to the orientation and coordination mode of the carboxylate ligand, which in turn is influenced by outer-sphere hydrogen bonding.
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