β-内酰胺酶II中锌配体的组氨酸残基。
Histidine residues of zinc ligands in beta-lactamase II.
作者信息
Baldwin G S, Galdes A, Hill H A, Smith B E, Waley S G, Abraham E P
出版信息
Biochem J. 1978 Nov 1;175(2):441-7. doi: 10.1042/bj1750441.
Abstract
- The Zn(II)-requiring beta-lactamase from Bacillus cereus 569/H/9, which has two zinc-binding sites, was examined by 270 MHz 1H n.m.r. spectroscopy. Resonances were assigned to five histidine residues. 2. Resonances attributed to three of the histidine residues in the apoenzyme shift on the addition of one equivalent of Zn(II). 3. Although these three histidine residues are free to titrate in the apoenzyme, none of them titrates over the pH range 6.0--9.0 in the mono-zinc enzyme. 4. The ability of the C-2 protons of these three histidine residues to exchange with solvent (2H2O) is markedly decreased on Zn(II) binding. 5. It is proposed that these three histidine residues act as zinc ligands at the tighter zinc-binding site. 6. Resonances attributed to a fourth histidine residue shift on addition of further zinc to the mono-zinc enzyme. It is proposed that this histidine residue acts as a Zn(II) ligand at the second zinc-binding site.
摘要
对来自蜡样芽孢杆菌569/H/9的需要锌（II）的β-内酰胺酶进行了270兆赫的1H核磁共振光谱研究，该酶有两个锌结合位点。共振信号被归属到五个组氨酸残基上。
在加入一当量的锌（II）后，脱辅基酶中三个组氨酸残基的共振信号发生位移。
虽然这三个组氨酸残基在脱辅基酶中可自由滴定，但在单锌酶中，它们在pH值6.0至9.0范围内均未发生滴定。
在锌（II）结合后，这三个组氨酸残基的C-2质子与溶剂（2H2O）交换的能力显著降低。
提出这三个组氨酸残基在较紧密的锌结合位点充当锌配体。
在向单锌酶中进一步加入锌后，第四个组氨酸残基的共振信号发生位移。提出这个组氨酸残基在第二个锌结合位点充当锌（II）配体。
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