Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
3P41RR002583-13S1
Application #
6319705
Study Section
Project Start
1998-05-05
Project End
2000-04-30
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
13
Fiscal Year
1999
Total Cost
Indirect Cost
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
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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
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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

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