G. Behravan

Publications16
h-index11
Citations518
Highly Influential Citations8
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Fine tuning of the catalytic properties of carbonic anhydrase. Studies of a Thr200----His variant of human isoenzyme II.
The active sites of carbonic anhydrases I contain a unique histidine residue at sequence position 200. To test the hypothesis that His200 is essential for the isoenzyme-specific catalytic and… Expand
  • 71
  • 2
Importance of the conserved active-site residues Tyr7, Glu106 and Thr199 for the catalytic function of human carbonic anhydrase II.
The catalytic mechanism of carbonic anhydrase includes the reaction of a zinc-bound hydroxide ion with the CO2 substrate. This hydroxide ion is part of a hydrogen-bonded network involving the… Expand
  • 62
  • 2
Evidence by site-directed mutagenesis supports long-range electron transfer in mouse ribonucleotide reductase.
Mammalian ribonucleotide reductase consists of two nonidentical subunits, proteins R1 and R2, each inactive alone. The R1 protein binds the ribonucleotide substrates while the R2 protein contains a… Expand
  • 83
  • 2
The solution structure of the homeodomain of the rat insulin-gene enhancer protein isl-1. Comparison with other homeodomains.
Homeodomains are one of the key families of eukaryotic DNA-binding motifs and provide an important model system for DNA recognition. We have determined a high-quality nuclear magnetic resonance (NMR)… Expand
  • 20
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Production of active human carbonic anhydrase II in E. coli.
cDNA encoding human carbonic anhydrase II has been isolated and its nucleotide sequence determined. Expression of the isolated carbonic anhydrase gene in Escherichia coli from a plasmid containing… Expand
  • 69
Histidine 64 is not required for high CO2 hydration activity of human carbonic anhydrase II
To test the hypothesis that histidine 64 in carbonic anhydrase II has a crucial role as a ‘proton shuttle group’ during catalysis of CO2‐HCO− 3 interconversion, this residue was replaced by lysine,… Expand
  • 38
Structural and functional differences between carbonic anhydrase isoenzymes I and II as studied by site-directed mutagenesis.
Site-specific mutagenesis has been used to replace amino acid residues in the active site of human carbonic anhydrase II with residues characterizing carbonic anhydrases I. Previous studies of… Expand
  • 47
Formation of a free radical of the sulfenylimine type in the mouse ribonucleotide reductase reaction with 2'-azido-2'-deoxycytidine 5'-diphosphate.
Mouse and Escherichia coli ribonucleotide reductases (RR) both belong to the same class of RR, where the enzyme consists of two non-identical subunits, proteins R1 and R2. A transient free radical… Expand
  • 11
The interaction of ellipticine derivatives with nucleic acids studied by optical and 1H‐nmr spectroscopy: Effect of size of the heterocyclic ring system
The DNA interaction of derivatives of ellipticine with heterocyclic ring systems with three, four, or five rings and a dimethylaminoethyl side chain was studied. Optical spectroscopy of drug… Expand
  • 29
Fine tuning of the catalytic properties of human carbonic anhydrase II. Effects of varying active-site residue 200.
The active-site residue Thr200 in human carbonic anhydrase II has been replaced by several different amino acids by site-directed mutagenesis. The CO2 hydration and 4-nitrophenyl acetate hydrolase… Expand
  • 17