A series of synthetic iron porphyrins are being prepared for the purpose of modelling the oxygen binding hemoproteins--hemoglobin, myoglobin, and cytochrome P-450. The structures of these synthetic models are being determined by X-ray diffraction and their physical properties (Mossbauer, electronic, and MCD spectra, magnetic moments, and vibrational spectra) are being determined for comparison with the natural hemoproteins. Special emphasis is being given to studies of models for the hydroxylase cytochrome P-450. Synthetic models for the low-spin and high-spin ferric and the ferrous carbonyl stages of P-450 have been characterized. Preparation and structural characterization of synthetic analogues of the deoxy ferrous form are progressing. Ruthenium analogues of these iron porphyrins are being prepared, including a dioxygen complex. A new """"""""capped"""""""" porphyrin and an extensive series of binary """"""""face-to-face"""""""" porphyrins have been prepared.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM017880-17
Application #
3563670
Study Section
(SSS)
Project Start
1977-12-01
Project End
1987-11-30
Budget Start
1986-12-01
Budget End
1987-11-30
Support Year
17
Fiscal Year
1987
Total Cost
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
Collman, James P; Ghosh, Somdatta (2010) Recent applications of a synthetic model of cytochrome c oxidase: beyond functional modeling. Inorg Chem 49:5798-810
Collman, James P; Ghosh, Somdatta; Dey, Abhishek et al. (2009) Using a functional enzyme model to understand the chemistry behind hydrogen sulfide induced hibernation. Proc Natl Acad Sci U S A 106:22090-5
Collman, James P; Ghosh, Somdatta; Dey, Abhishek et al. (2009) Catalytic reduction of O2 by cytochrome C using a synthetic model of cytochrome C oxidase. J Am Chem Soc 131:5034-5
Collman, James P; Dey, Abhishek; Yang, Ying et al. (2009) O2 reduction by a functional heme/nonheme bis-iron NOR model complex. Proc Natl Acad Sci U S A 106:10528-33
Collman, James P; Decréau, Richard A; Lin, Hengwei et al. (2009) Role of a distal pocket in the catalytic O2 reduction by cytochrome c oxidase models immobilized on interdigitated array electrodes. Proc Natl Acad Sci U S A 106:7320-3
Collman, James P; Dey, Abhishek; Barile, Christopher J et al. (2009) Inhibition of electrocatalytic O(2) reduction of functional CcO models by competitive, non-competitive, and mixed inhibitors. Inorg Chem 48:10528-34
Collman, James P; Decreau, Richard A; Dey, Abhishek et al. (2009) Water may inhibit oxygen binding in hemoprotein models. Proc Natl Acad Sci U S A 106:4101-5
Collman, James P; Dey, Abhishek; Decreau, Richard A et al. (2008) Model studies of azide binding to functional analogues of CcO. Inorg Chem 47:2916-8
Collman, James P; Decreau, Richard A (2008) Functional biomimetic models for the active site in the respiratory enzyme cytochrome c oxidase. Chem Commun (Camb) :5065-76
Collman, James P; Dey, Abhishek; Decreau, Richard A et al. (2008) Interaction of nitric oxide with a functional model of cytochrome c oxidase. Proc Natl Acad Sci U S A 105:9892-6

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