大肠杆菌杂交簇蛋白的羟胺还原酶活性
Hydroxylamine reductase activity of the hybrid cluster protein from Escherichia coli.
作者信息
Wolfe Marcus T, Heo Jongyun, Garavelli John S, Ludden Paul W
机构信息
Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison, Madison, WI 53706, USA.
出版信息
J Bacteriol. 2002 Nov;184(21):5898-902. doi: 10.1128/JB.184.21.5898-5902.2002.
Abstract
The hybrid cluster protein (HCP; formerly termed the prismane protein) has been extensively studied due to its unique spectroscopic properties. Although the structural and spectroscopic characteristics are well defined, its enzymatic function, up to this point, has remained unidentified. While it was proposed that HCP acts in some step of nitrogen metabolism, a specific role for this enzyme remained unknown. Recent studies of HCP purified from Escherichia coli have identified a novel hydroxylamine reductase activity. These data reveal the ability of HCP to reduce hydroxylamine in vitro to form NH(3) and H(2)O. Further biochemical analyses were completed in order to determine the effects of various electron donors, different pH levels, and the presence of CN(-) on in vitro hydroxylamine reduction.
摘要
杂合簇蛋白（HCP；以前称为棱柱烷蛋白）因其独特的光谱性质而受到广泛研究。尽管其结构和光谱特征已得到明确界定，但到目前为止，其酶功能仍未确定。虽然有人提出HCP在氮代谢的某些步骤中起作用，但该酶的具体作用仍然未知。最近对从大肠杆菌中纯化的HCP的研究确定了一种新的羟胺还原酶活性。这些数据揭示了HCP在体外将羟胺还原形成NH(3)和H(2)O的能力。为了确定各种电子供体、不同pH水平以及CN(-)的存在对体外羟胺还原的影响，进一步完成了生化分析。
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