XAS studies of Ni(I), Ni(II), and Ni(III) complexes
نویسندگان
چکیده
منابع مشابه
Geometric and Electronic Structures of the NiI and Methyl−NiIII Intermediates of Methyl-Coenzyme M Reductase†
Methyl-coenzyme M reductase (MCR) catalyzes the terminal step in the formation of biological methane from methyl-coenzyme M (Me-SCoM) and coenzyme B (CoBSH). The active site in MCR contains a Ni-F(430) cofactor, which can exist in different oxidation states. The catalytic mechanism of methane formation has remained elusive despite intense spectroscopic and theoretical investigations. On the bas...
متن کاملpostnatal studies of bats (pipistrellus kuhlii and miniopterus schreibersii) & histomorphology and histochemistry studies of organs and diseases of (neurergus microspilotus and n. kaiseri)
1. to determine whether difference in birth body mass influenced growth performance in pipistrellus kuhlii we studied a total of 12 captive-born neonates. bats were assigned to two body mass groups: light birth body mass (lbw: 0.89 ± 0.05, n=8) and heavy birth body mass (hbw: 1.35 ± 0.08, n=4). heavier body mass at birth was associated with rapid postnatal growth (body mass and forearm length) ...
synthesis and dna interaction studies of new cobalt (ii) complexes containing different dinitrogen aaromatic ligands with calf thymus dna using different spectroscopy methods
در این مطالعه بر هم کنش این چهار کمپلکس با dna تیموس گوساله توسط روش های اسپکتروفتومتری، فلوریمتری، دو رنگ نمائی دورانی، و ویسکوزیمتری بررسی شدند تا اثر استخلاف های متیل بر روی لیگاندهای فنانترولین بررسی گردد.
Time-dependent XAS studies of trapped enzyme-substrate complexes of alcohol dehydrogenase from Thermoanaerobacter brockii.
The understanding of structure-function relationships in proteins has been significantly advanced with the advent of the biotechnological revolution. A goal yet to be realized for many metalloenzyme systems is to characterize the dynamic changes in structure that bridge the static endpoints provided by crystallography. We present here a series of edge and EXAFS spectra of the metalloenzyme alco...
متن کاملMononuclear nickel(II)-superoxo and nickel(III)-peroxo complexes bearing a common macrocyclic TMC ligand.
Mononuclear metal-dioxygen adducts, such as metal-superoxo and -peroxo species, are generated as key intermediates in the catalytic cycles of dioxygen activation by heme and non-heme metalloenzymes. We have shown recently that the geometric and electronic structure of the Ni-O2 core in [Ni(n-TMC)(O2)]+ (n = 12 and 14) varies depending on the ring size of the supporting TMC ligand. In this study...
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ژورنال
عنوان ژورنال: Physica B: Condensed Matter
سال: 1995
ISSN: 0921-4526
DOI: 10.1016/0921-4526(94)01040-8