Aconitase as iron− sulfur protein, enzyme, and iron-regulatory protein

H Beinert, MC Kennedy, CD Stout - Chemical reviews, 1996 - ACS Publications
Sixty years ago Carl Martius (1906-1993), then “Wissenschaftlicher Assistent” to Franz
Knoop at the Biochemical Institute of the University of Tubingen, did an experiment, crucial …

NAD (+)-dependent formate dehydrogenase.

VO Popov, VS Lamzin - Biochemical Journal, 1994 - ncbi.nlm.nih.gov
NAD (P)+-dependent dehydrogenases comprise a substantial and diverse group of proteins
differing in structure and function. They catalyse a number of key metabolic steps and …

Low-barrier hydrogen bonds and enzymic catalysis

WW Cleland, MM Kreevoy - Science, 1994 - science.org
Formation of a short (less than 2.5 angstroms), very strong, low-barrier hydrogen bond in the
transition state, or in an enzyme-intermediate complex, can be an important contribution to …

Malate dehydrogenase: a model for structure, evolution, and catalysis

CR Goward, DJ Nicholls - Protein Science, 1994 - Wiley Online Library
Malate dehydrogenases are widely distributed and alignment of the amino acid sequences
show that the enzyme has diverged into 2 main phylogenetic groups. Multiple amino acid …

A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework

HM Wilks, KW Hart, R Feeney, CR Dunn, H Muirhead… - Science, 1988 - science.org
Three variations to the structure of the nicotinamide adenine dinucleotide (NAD)-dependent
L-lactate dehydrogenase from Bacillus stearothermophilus were made to try to change the …

Molecular structure of flavocytochrome b2 at 24 Å resolution

Z Xia, FS Mathews - Journal of molecular biology, 1990 - Elsevier
The crystal structure of flavocytochrome b 2 has been solved at 3.0 Å resolution by the
method of multiple isomorphous replacement with anomalous scattering. Area detector data …

Protein heterozygosity, protein structure, and taxonomic differentiation

RD Ward, DOF Skibinski, M Woodwark - Evolutionary Biology: Volume 26, 1992 - Springer
Soon after the introduction of electrophoretic techniques to study the genetic structure of
natural populations of animals and plants came the realization that enzymes differed in their …

The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase

DJ Schuller, GA Grant, LJ Banaszak - Nature structural biology, 1995 - nature.com
The crystal structure of the phosphoglycerate dehydrogenase from Eschehchia coli is
unique among dehydrogenases. It consists of three clearly separate domains connected by …

Identification of native protein folds amongst a large number of incorrect models: the calculation of low energy conformations from potentials of mean force

M Hendlich, P Lackner, S Weitckus, H Floeckner… - Journal of molecular …, 1990 - Elsevier
We present an approach that is able to detect native folds amongst a large number of non-
native conformations. The method is based on the compilation of potentials of mean force of …

High resolution structures of holo and apo formate dehydrogenase

VS Lamzin, Z Dauter, VO Popov… - Journal of molecular …, 1994 - Elsevier
Three-dimensional crystal structures of holo (ternary complex enzyme-NAD-azide) and apo
NAD-dependent dimeric formate dehydrogenase (FDH) from the methylotrophic bacterium …