The mutation Met121-->His creates a type-1.5 copper site in Alcaligenes denitrificans azurin.
The mutation Met121-->His creates a type-1.5 copper site in Alcaligenes denitrificans azurin.
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突变 Met121-->His 在产碱杆菌天青蛋白中产生了 1.5 型铜位点。
DOI:
10.1111/j.1432-1033.1996.0342h.x
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发表时间:
1996
期刊:
影响因子:
--
通讯作者:
Canters,GW
中科院分区:
文献类型:
--
作者:
Kroes,SJ;Hoitink,CW;Andrew,CR;Ai,J;Sanders-Loehr,J;Messerschmidt,A;Hagen,WR;Canters,GW
The Cu ligand Met121 in azurin ofAlcaligenes denitrificanswas mutated to His. The spectroscopic and mechanistic properties of [M121H]azurin appear to be pH dependent with a pKaof 3.8 due to the ionization of His121. The [M121H]azurin mutant exhibits two major distinct metal‐site‐coordination geometries which coexist in solution according to a pH‐dependent equilibrium. Both species have been spectroscopically characterized by ultraviolet–visible, EPR and resonance Raman spectroscopies. At neutral pH, His121 is deprotonated and acts as the fourth ligand of the Cu; the spectroscopic characteristics of the Cu site at this pH are halfway between those of a type‐1 and a type‐2 Cu site, and the site is referred to as a type‐1.5 or intermediate Cu site. The spectral data are compatible with a tetrahedral geometry of this site. At low pH, the spectroscopic data indicate that [M121H]azurin has a trigonal type‐1 rhombic Cu site.
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DOI:
--
发表时间:
1976
期刊:
影响因子:
--
作者:
長島 弘幸
通讯作者:
長島 弘幸
DOI:
--
发表时间:
1977
期刊:
Biochemical and Biophysical Research Communications - BBRC
影响因子:
--
作者:
Claes Bergman;E. Gandvik;Per Olof Nyman;Lars Strid
通讯作者:
Lars Strid
影响因子:
--
作者:
E. Adman
通讯作者:
E. Adman
DOI:
10.1016/s0021-9258(19)49644-0
发表时间:
1992
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
C. Hoitink;G. Canters
通讯作者:
G. Canters
影响因子:
3.9
作者:
C. Groeneveld;R. Aasa;B. Reinhammar;G. Canters
通讯作者:
G. Canters