Iron-catalyzed atom transfer radical polymerization

Z Xue, D He, X Xie - Polymer Chemistry, 2015 - pubs.rsc.org
In the last two decades, metal-catalyzed controlled radical polymerization (CRP), or atom
transfer radical polymerization (ATRP) has become a ubiquitous tool for the facile synthesis …

[图书][B] Chemical reagents for protein modification

RL Lundblad - 2004 - taylorfrancis.com
Revised and updated, Chemical Reagents for Protein Modification, Third Edition is an
encyclopedic work describing the many approaches to the site-specific modification of …

Automatic determination of disulfide bridges in proteins

I Sokolowska, AG Ngounou Wetie… - Journal of …, 2012 - journals.sagepub.com
Precise determination of disulfide linkages between cysteine (Cys) residues in proteins is
essential in the determination of protein structure. Therefore, a reliable automated method …

Mechanistic implications of persulfenate and persulfide binding in the active site of cysteine dioxygenase

RJ Souness, T Kleffmann, EP Tchesnokov… - Biochemistry, 2013 - ACS Publications
Describing the organization of substrates and substrate analogues in the active site of
cysteine dioxygenase identifies potential intermediates in this critical yet poorly understood …

Lack of conventional oxygen-linked proton and anion binding sites does not impair allosteric regulation of oxygen binding in dwarf caiman hemoglobin

RE Weber, A Fago, H Malte… - American Journal of …, 2013 - journals.physiology.org
In contrast to other vertebrate hemoglobins (Hbs) whose high intrinsic O2 affinities are
reduced by red cell allosteric effectors (mainly protons, CO2, organic phosphates, and …

Insertion of Heme b into the Structure of the Cys34‐Carbamidomethylated Human Lipocalin α1‐Microglobulin: Formation of a [(Heme)21‐Microglobulin)]3 …

JF Siebel, RL Kosinsky, B Åkerström, M Knipp - Chembiochem, 2012 - Wiley Online Library
Abstract α1‐Microglobulin (α1m) is a 26 kDa plasma and tissue protein belonging to the
lipocalin protein family. Previous investigations indicate that the protein interacts with heme …

[HTML][HTML] Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7

M Knipp, H Ogata, G Soavi, G Cerullo, A Allegri… - …, 2015 - ncbi.nlm.nih.gov
Nitrophorins represent a unique class of heme proteins that are able to perform the delicate
transportation and release of the free-radical gaseous messenger nitric oxide (NO) in a pH …

Heterogeneous kinetics of the carbon monoxide association and dissociation reaction to nitrophorin 4 and 7 coincide with structural heterogeneity of the gate-loop

S Abbruzzetti, C He, H Ogata, S Bruno… - Journal of the …, 2012 - ACS Publications
NO is an important signaling molecule in human tissue. However, the mechanisms by which
this molecule is controlled and directed are currently little understood. Nitrophorins (NPs) …

Breaking the Proximal FeII–NHis Bond in Heme Proteins through Local Structural Tension: Lessons from the Heme b Proteins Nitrophorin 4, Nitrophorin 7, and …

C He, S Neya, M Knipp - Biochemistry, 2011 - ACS Publications
The factors leading to the breakage of the proximal iron–histidine bond in the ferroheme
protein soluble guanylate cyclase (sGC) are still a matter of debate. This event is a key …

Identification of residues in the heme domain of soluble guanylyl cyclase that are important for basal and stimulated catalytic activity

P Baskaran, EJ Heckler, F van den Akker, A Beuve - PloS one, 2011 - journals.plos.org
Nitric oxide signals through activation of soluble guanylyl cyclase (sGC), a heme-containing
heterodimer. NO binds to the heme domain located in the N-terminal part of the β subunit of …