PAH when reduced, reacts with NO. The EPR, extending from g = 4 to g = 2 is indicative of an S = 3/2 system. The cw EPR is perturbed by either substrate or pterin addition. ESEEM studies show weak modulations from 14N that disappear in samples that are allowed to anneal. Studies to be carried out will be addressed at demonstrating interaction with substrate and/or cofactors using deuterated materials.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR002583-13
Application #
6281734
Study Section
Project Start
1998-05-05
Project End
2000-04-30
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
13
Fiscal Year
1998
Total Cost
Indirect Cost
Name
Albert Einstein College of Medicine
Department
Type
DUNS #
009095365
City
Bronx
State
NY
Country
United States
Zip Code
10461
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
Magliozzo, R S; Bubacco, L; McCracken, J et al. (1995) Cu(II) coordination in arthropod and mollusk green half-methemocyanins analyzed by electron spin-echo envelope modulation spectroscopy. Biochemistry 34:1513-23
Marcinkeviciene, J A; Magliozzo, R S; Blanchard, J S (1995) Purification and characterization of the Mycobacterium smegmatis catalase-peroxidase involved in isoniazid activation. J Biol Chem 270:22290-5

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