Abstract

EPR studies of soybean leghemoglobin a (Lb) in the presence of perfluorophenol(PF) or paranitrophenol,(PN) and of Paramphistomum epiclitum hemoglobin have been conducted. This Hb contains two tyr residues in their distal pockets, at positions B10 and at E7. With phenols, Lb exists as high spin/low spin mixtures. The g = of 2.73, 2.26, 1.75 and 2.64, 2.22, 1.80 for the low spin forms with PF and PN, respectively. This spin mixture property is analogous to hemoproteins with known ligation such as Hbn M and Lucina pectinata HbII. The g values for the low spin form of Lb in the presence of PF resemble those resolved for the proposed hist-tyr complex of L. pectinata Hb II (2.76, 1.75), while the g values for low spin Lb in the presence of PN resemble those of the proposed OH complex of L. pectinata Hb II (2.61, 2.20, 1.82). P. epiclitumIn Hb exhibits high spin-low spin mixture at alkaline pH (9.3). The low spin forms has g values of 2.67, 2.13, 1.78. The increased anisotropy as compared to the HO complexes of L. pectinata Hb II (g=2.61, 2.20, 1.82) and myoglobin (2.55, 2.17, 1.85) suggest tyr coordination to the heme Fe. It is suggested that the E7 tyrosine of P. epiclitumIn Hb serves as an axial heme ligand. ?

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
3P41RR002583-13S1
Application #
6121167
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

  Institution

Name
Albert Einstein College of Medicine
Department
Type
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
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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
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

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