作者
Katrin Fischer, Angel Llamas, Manuel Tejada-Jimenez, Nils Schrader, Jochen Kuper, Farid S Ataya, Aurora Galvan, Ralf R Mendel, Emilio Fernandez, Guenter Schwarz
发表日期
2006/10/6
期刊
Journal of biological chemistry
卷号
281
期号
40
页码范围
30186-30194
出版商
Elsevier
简介
The molybdenum cofactor (Moco) forms the catalytic site in all eukaryotic molybdenum enzymes and is synthesized by a multistep biosynthetic pathway. The mechanism of transfer, storage, and insertion of Moco into the appropriate apo-enzyme is poorly understood. In Chlamydomonas reinhardtii, a Moco carrier protein (MCP) has been identified and characterized recently. Here we show biochemical evidence that MCP binds Moco as well as the tungstate-substituted form of the cofactor (Wco) with high affinity, whereas molybdopterin, the ultimate cofactor precursor, is not bound. This binding selectivity points to a specific metal-mediated interaction with MCP, which protects Moco and Wco from oxidation with t½ of 24 and 96 h, respectively. UV-visible spectroscopy showed defined absorption bands at 393, 470, and 570 nm pointing to ene-diothiolate and protein side-chain charge transfer bonds with molybdenum …
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K Fischer, A Llamas, M Tejada-Jimenez, N Schrader… - Journal of biological chemistry, 2006