CO as a vibrational probe of heme protein active sites
TG Spiro, IH Wasbotten - Journal of inorganic biochemistry, 2005 - Elsevier
Carbon monoxide is a useful vibrational probe of heme binding sites in proteins, because
FeCO backbonding is modulated by polar interactions with protein residues, and by …
FeCO backbonding is modulated by polar interactions with protein residues, and by …
Probing the structure and bifunctionality of catalase-peroxidase (KatG)
G Smulevich, C Jakopitsch, E Droghetti… - Journal of inorganic …, 2006 - Elsevier
Catalase-peroxidases (KatGs) exhibit peroxidase and substantial catalase activities similar
to monofunctional catalases. Crystal structures of four different KatGs reveal the presence of …
to monofunctional catalases. Crystal structures of four different KatGs reveal the presence of …
[图书][B] Handbook Of Porphyrin Science: With Applications To Chemistry, Physics, Materials Science, Engineering, Biology And Medicine (Volumes 6-10)
This is the second set of Handbook of Porphyrin Science. Porphyrins, phthalocyanines and
their numerous analogues and derivatives are materials of tremendous importance in …
their numerous analogues and derivatives are materials of tremendous importance in …
The Asp-His-iron triad of cytochrome c peroxidase controls the reduction potential electronic structure, and coupling of the tryptophan free radical to the heme
Revised Manuscript Received December 18, 1992 abstract: The buried charge of Asp-235
in cytochrome c peroxidase (CCP) forms an important hydrogen bond to the histidine ligand …
in cytochrome c peroxidase (CCP) forms an important hydrogen bond to the histidine ligand …
How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and models
GB Ray, XY Li, JA Ibers, JL Sessler… - Journal of the American …, 1994 - ACS Publications
Resonance Raman (RR) spectra are reported for structurally defined CO adducts of two
sterically constrained Fe11 porphyrins: PocPiv, in which three of the pivaloylamino pickets of …
sterically constrained Fe11 porphyrins: PocPiv, in which three of the pivaloylamino pickets of …
Structural Interactions between Horseradish Peroxidase C and the Substrate Benzhydroxamic Acid Determined by X-ray Crystallography,
A Henriksen, DJ Schuller, K Meno, KG Welinder… - Biochemistry, 1998 - ACS Publications
The three-dimensional structure of recombinant horseradish peroxidase in complex with
BHA (benzhydroxamic acid) is the first structure of a peroxidase− substrate complex …
BHA (benzhydroxamic acid) is the first structure of a peroxidase− substrate complex …
Structures of the Siroheme- and Fe4S4-Containing Active Center of Sulfite Reductase in Different States of Oxidation: Heme Activation via Reduction-Gated Exogenous …
BR Crane, LM Siegel, ED Getzoff - Biochemistry, 1997 - ACS Publications
The active center of the Escherichia coli sulfite reductase hemoprotein (SiRHP) is exquisitely
designed to catalyze the six-electron reductions of sulfite to sulfide and nitrite to ammonia …
designed to catalyze the six-electron reductions of sulfite to sulfide and nitrite to ammonia …
Mutation of distal residues of horseradish peroxidase: influence on substrate binding and cavity properties
BD Howes, JN Rodriguez-Lopez, AT Smith… - Biochemistry, 1997 - ACS Publications
The manner in which the distal heme pocket residues of peroxidases control the reaction
mechanism and ligand binding has been investigated further by analysis of the electronic …
mechanism and ligand binding has been investigated further by analysis of the electronic …
Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: what have we learned?
G Smulevich, A Feis, BD Howes - Accounts of chemical research, 2005 - ACS Publications
Spectroscopic techniques have been fundamental to the comprehension of peroxidase
function under physiological conditions. This Account examines the contribution to our …
function under physiological conditions. This Account examines the contribution to our …
How active-site protonation state influences the reactivity and ligation of the heme in chlorite dismutase
BR Streit, B Blanc, GS Lukat-Rodgers… - Journal of the …, 2010 - ACS Publications
Chlorite dismutase catalyzes O2 release from chlorite with exquisite efficiency and
specificity. The spectroscopic properties, ligand binding affinities, and steady-state kinetics …
specificity. The spectroscopic properties, ligand binding affinities, and steady-state kinetics …