Electronic structure of the iron-molybdenum and alternative cofactors of nitrogenases: a comparison and its consequences
References (34)
- et al.
- et al.
program package CACAO
J. Chem. Educ.
(1990) - et al.
Am. Rev. Biochem.
(1984) Chem. Rev.
(1993)- et al.
Biochemistry
(1986) - et al.
Biochem. J.
(1987) - et al.
J. Bacteriol.
(1989) - et al.
Eur. J. Biochem.
(1991)
Biochem. J.
Biochem. J.
Eur. J. Biochem.
Biochem. J.
Cited by (32)
Structure and electrochemistry of proteins harboring iron-sulfur clusters of different nuclearities. Part V. Nitrogenases
2019, Coordination Chemistry ReviewsCitation Excerpt :Such an enzyme is also commonly known as “Fe-only nitrogenase” or as “nitrogenase 3” (representatively [15,35,185–187]). Since at moment no pertinent crystallographic data is available, but for a few theoretical calculations [188–191] focussed on the plausible similarity of the molecular structures of MFe cofactors (M = Mo, V, Fe), this argument would have to be excluded from the present review paper. Nevertheless a minimum knowledge of the basics of such a topic can be useful.
Vanadium(V) complex with Schiff-base ligand containing a flexible amino side chain: Synthesis, structure and reactivity
2015, Journal of Inorganic BiochemistryCitation Excerpt :The continuous interest in vanadium coordination chemistry is particularly due to its ability to catalyze various oxidation reactions [1–4], as well as its presence in biological systems like in certain vanadium-dependent haloperoxidase (VHPO) enzymes [5] and nitrogenases [6,7].
Vanadium complexes with side chain functionalized N-salicylidene hydrazides: Hydrogen-bonding relays as structural directive for supramolecular interactions
2014, Inorganica Chimica ActaCitation Excerpt :The continuous interest in the coordination chemistry of vanadium is based on the wide range of biological and catalytic properties in relevant systems [1–5]. Besides the insulin-like effect of vanadium compounds [6], this is related to the presence of vanadium in certain haloperoxidases [7] and nitrogenases [8,9]. A key point for the understanding of the mode of action of vanadium in biological systems is given by the chemical analogy between vanadates and phosphates [10].
Nitrogenase and Nitrogen Activation
2013, Comprehensive Inorganic Chemistry II (Second Edition): From Elements to ApplicationsChiral and supramolecular model complexes for vanadium haloperoxidases: Host-guest systems and hydrogen bonding relays for vanadate species
2011, Coordination Chemistry ReviewsCitation Excerpt :There is continuous interest in the coordination chemistry of vanadium due to the biological and catalytic properties of relevant systems [1–8]. Besides the discovery of the insulin-like effect of vanadium compounds, this is related to the presence of vanadium in certain haloperoxidases [9] and nitrogenases [10,11]. Vanadium haloperoxidases are enzymes that catalyze different oxidation reactions like the oxidation of halides to corresponding hypohalous acids and the oxidation of organic sulfides to sulfoxides [12–14].
QUANTUM CHEMICAL INVESTIGATIONS INTO THE PROBLEM OF BIOLOGICAL NITROGEN FIXATION: SELLMANN-TYPE METAL-SULFUR MODEL COMPLEXES
2004, Advances in Inorganic ChemistryCitation Excerpt :Pioneering studies with semi-empirical methods were carried out shortly after the discovery of the FeMoco structure via X-ray diffraction experiments (21,22). These extended-Hückel calculations have been carried out for structurally fixed models of FeMoco (23,24) and of FeMoco, FeVco, and FeFeco (25), in which the three amino acid ligands have been replaced by hydride ligands. The main results of these studies are deduced based on the assumption that the character of the frontier orbitals, i.e., their composition in terms of atomic orbitals, determines the binding of dinitrogen.