Murphy L M, Strange R W, Karlsson B G, Lundberg L G, Pascher T, Reinhammar B, Hasnain S S
Molecular Biophysics Group, Daresbury Laboratory, Warrington, Cheshire, U.K.
Biochemistry. 1993 Mar 2;32(8):1965-75. doi: 10.1021/bi00059a013.
Azurin from Pseudomonas aeruginosa and two mutants where the methionine ligand has been mutated have been studied in order to directly investigate the functional and structural significance of this ligand in the blue copper proteins. Reduction potentials, X-ray absorption fine structure (XAFS), electron paramagnetic resonance (EPR), and optical spectra are obtained in an attempt to provide a direct correlation between the spectrochemical properties and the immediate structure of this redox center.
对来自铜绿假单胞菌的天青蛋白以及甲硫氨酸配体发生突变的两个突变体进行了研究，以便直接探究该配体在蓝铜蛋白中的功能和结构意义。通过测定还原电位、X射线吸收精细结构（XAFS）、电子顺磁共振（EPR）和光谱，试图在该氧化还原中心的光谱化学性质与其直接结构之间建立直接关联。
