Dioxygen activation by nonheme diiron enzymes: diverse dioxygen adducts, high-valent intermediates, and related model complexes

AJ Jasniewski, L Que Jr - Chemical Reviews, 2018 - ACS Publications
A growing subset of metalloenzymes activates dioxygen with nonheme diiron active sites to
effect substrate oxidations that range from the hydroxylation of methane and the …

Calcineurin: form and function

F Rusnak, P Mertz - Physiological reviews, 2000 - journals.physiology.org
Calcineurin is a eukaryotic Ca2+-and calmodulin-dependent serine/threonine protein
phosphatase. It is a heterodimeric protein consisting of a catalytic subunit calcineurin A …

A multiplet analysis of Fe K-edge 1s→ 3d pre-edge features of iron complexes

TE Westre, P Kennepohl, JG DeWitt… - Journal of the …, 1997 - ACS Publications
X-ray absorption Fe− K edge data on ferrous and ferric model complexes have been studied
to establish a detailed understanding of the 1s→ 3d pre-edge feature and its sensitivity to …

Binuclear metallohydrolases

DE Wilcox - Chemical Reviews, 1996 - ACS Publications
Metabolic and signaling biochemical pathways have numerous steps that involve the
hydrolytic cleavage of peptide or phosphate ester bonds. Although both types of bonds are …

The catalytic mechanisms of binuclear metallohydrolases

N Mitić, SJ Smith, A Neves, LW Guddat… - Chemical …, 2006 - ACS Publications
Binuclear metallohydrolases are a structurally diverse group of enzymes that use binuclear
metal ion centers to catalyze the hydrolysis of amides and esters of carboxylic and …

Two‐metal ion catalysis in enzymatic Acyl‐and phosphoryl‐transfer reactions

N Sträter, WN Lipscomb, T Klabunde… - … International Edition in …, 1996 - Wiley Online Library
Numerous studies, both in enzymatic and nonenzymatic catalysis, have been undertaken to
understand the way by which metal ions, especially zinc ions, promote the hydrolysis of …

Mechanism of Fe (III)–Zn (II) purple acid phosphatase based on crystal structures

T Klabunde, N Sträter, R Fröhlich, H Witzel… - Journal of molecular …, 1996 - Elsevier
Purple acid phosphatase is a widely distributed non-specific phosphomonoesterase. X-ray
structures of the dimeric 111-kDa Fe (III)-Zn (II) kidney bean purple acid phosphatase …

Crystal structure of a purple acid phosphatase containing a dinuclear Fe (III)-Zn (II) active site

N Sträter, T Klabunde, P Tucker, H Witzel, B Krebs - Science, 1995 - science.org
Kidney bean purple acid phosphatase (KBPAP) is an Fe (III)-Zn (II) metalloenzyme
resembling the mammalian Fe (III)-Fe (II) purple acid phosphatases. The structure of the …

Absence of Mn-Centered Oxidation in the S2 → S3 Transition:  Implications for the Mechanism of Photosynthetic Water Oxidation

J Messinger, JH Robblee, U Bergmann… - Journal of the …, 2001 - ACS Publications
A key question for the understanding of photosynthetic water oxidation is whether the four
oxidizing equivalents necessary to oxidize water to dioxygen are accumulated on the four …

Structural and functional studies on model compounds of purple acid phosphatases and catechol oxidases

R Than, AA Feldmann, B Krebs - Coordination Chemistry Reviews, 1999 - Elsevier
The synthesis, single crystal X-ray crystallographic, magnetic and electrochemical
characterization of eight representative symmetric and unsymmetric complexes as structural …