18 Equilibrium Isotope Effects in Fe & CO Containing Hemoproteins

Abstract

Discussion of how 18O equilibrium isotope effect is related to O2 affinity and H-bonding in Fe and Co containing hemoglobins and myoglobins. A mechanism for the Bohr effect is suggested which entails a reductio of H-boding to bound O2 brought about by alteration in protein structure.

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Center for Research Resources (NCRR)
• Type: Biotechnology Resource Grants (P41)
• Project #: 2P41RR002583-12
• Application #: 2548924
• Budget Start: 1996-10-01
• Budget End: 1997-09-30
• Support Year: 12
• Fiscal Year: 1997

Institution

• Name: Albert Einstein College of Medicine
• DUNS #: 009095365
• City: Bronx
• State: NY
• Country: United States
• Zip Code: 10461

Publications

Colaneri, M J; Vitali, J; Peisach, J (2000) Electron spin-echo envelope modulation study of multicrystalline Cu(2+)-insulin: effects of Cd(2+) on the nuclear quadrupole interaction of the Cu(2+)-coordinated imidazole remote nitrogen. Biochemistry 39:584-91

Lee, H C; Goroncy, A K; Peisach, J et al. (2000) Demonstration of a conserved histidine and two water ligands at the Mn2+ site in Diocleinae lectins by pulsed EPR spectroscopy. Biochemistry 39:2340-6

Sam, J W; Takahashi, S; Lippai, I et al. (1998) Sequence-specific changes in the metal site of ferric bleomycin induced by the binding of DNA. J Biol Chem 273:16090-7

Magliozzo, R S; Marcinkeviciene, J A (1997) The role of Mn(II)-peroxidase activity of mycobacterial catalase-peroxidase in activation of the antibiotic isoniazid. J Biol Chem 272:8867-70

Nersissian, A M; Mehrabian, Z B; Nalbandyan, R M et al. (1996) Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form. Protein Sci 5:2184-92

Gasdaska, J R; Law, J H; Bender, C J et al. (1996) Cockroach transferrin closely resembles vertebrate transferrins in its metal ion-binding properties: a spectroscopic study. J Inorg Biochem 64:247-58

Tipton, P A; Quinn, T P; Peisach, J et al. (1996) Role of the divalent metal ion in the NAD:malic enzyme reaction: an ESEEM determination of the ground state conformation of malate in the E:Mn:malate complex. Protein Sci 5:1648-54

Coffino, A R; Peisach, J (1996) Simulation of Mn (II) EPR spectra using a full spin-Hamiltonian approach. J Magn Reson B 111:127-34

Parast, C V; Wong, K K; Lewisch, S A et al. (1995) Hydrogen exchange of the glycyl radical of pyruvate formate-lyase is catalyzed by cysteine 419. Biochemistry 34:2393-9

Theodorakis, J L; Garber, E A; McCracken, J et al. (1995) A chemical modification of cytochrome-c lysines leading to changes in heme iron ligation. Biochim Biophys Acta 1252:103-13