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• W2909993685 abstract "This chapter deals with the chemical systems designed to reproduce aspects of the structure and function of the nitrogenase enzymes. The X-ray crystal structural data for the active metal centers of molybdenum nitrogenase are discussed. The three known types of nitrogenase consist of two readily separable, oxygen-sensitive proteins. One is a relatively small α 2 -type protein which contains a single {Fe 4 S 4 (cysteinyl) 4 } and acts as an electron donor to the second, larger α 2 β 2 -type protein. The geometry of the six apparently three-coordinate iron atoms at the center of the FeMoco cluster might be described as tending towards trigonal pyramidal, rather than trigonal planar, since each of the Fe atoms is displaced below the S 3 plane and towards the center of the cluster by a mean distance of around 0.051 nm. FeMoco can be isolated from the Mo–Fe protein in N–methylformamide solution, when it then has lost the binding of the terminal Fe to cysteine and the histidine to the Mo. It is normally isolated in the so-called semi-reduced state and although it has not been shown to interact with N 2 in this condition, its reactions with a number of other nitrogenase substrates have been investigated. The binding of CN - has been investigated by a combination of spectroscopic techniques, including X-ray absorption fine structure analysis. Cyanide appears to bind to both Fe and Mo; competitive binding between thiolate and CN - seems to result in the terminal Fe being bound by thiolate and the Mo by CN - ." @default.
• W2909993685 created "2019-01-25" @default.
• W2909993685 creator A5063650169 @default.
• W2909993685 date "2002-01-01" @default.
• W2909993685 modified "2023-10-14" @default.
• W2909993685 title "Chemical Models for Nitrogenase" @default.
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