Michael F. Davis

发表

Evaluation of emissions from remedial activity at a former manufactured gas plant by open-path Fourier transform infrared spectroscopy

Robert M. Hammaker, William G. Fateley, Michael F. Davis, 1995, Other Conferences.

Estimation of VOC emission rates from FTIR measurements and whole-air canister data

Robert M. Hammaker, William G. Fateley, Michael F. Davis, 1995, Other Conferences.

Different modes of binding of mono-, di-, and trihalogenated phenols to the hemoglobin dehaloperoxidase from Amphitrite ornata.

Michael F. Davis, Franck A. P. Vendeix, S. Franzen, 2009, Biochemistry.

Determinants of substrate internalization in the distal pocket of dehaloperoxidase hemoglobin of Amphitrite ornata.

Michael F. Davis, G. Nienhaus, K. Nienhaus, 2008, Biochemistry.

X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned from Amphitrite ornata.

Michael F. Davis, S. Franzen, V. de Serrano, 2008, Acta crystallographica. Section D, Biological crystallography.

Internal binding of halogenated phenols in dehaloperoxidase-hemoglobin inhibits peroxidase function.

Michael F. Davis, S. Franzen, B. Howes, 2010, Biophysical journal.

Detection of Ras GTPase protein radicals through immuno-spin trapping.

Michael F. Davis, Xian Chen, H. Gunawardena, 2012, Free radical biology & medicine.

Dehaloperoxidase-hemoglobin from Amphitrite ornata is primarily a monomer in solution.

Michael F. Davis, S. Franzen, R. Oliver, 2011, The journal of physical chemistry. B.

Regulation of Ras proteins by reactive nitrogen species.

Michael F. Davis, D. Vigil, S. Campbell, 2011, Free radical biology & medicine.

Laser flash photolysis studies of intramolecular electron transfer in milk xanthine oxidase

Michael F. Davis, G. Tollin, A. Bhattacharyya, 1983 .

Enzyme function of the globin dehaloperoxidase from Amphitrite ornata is activated by substrate binding.

Michael F. Davis, M. Godek, S. Franzen, 2005, Biochemistry.

Proximal cavity, distal histidine, and substrate hydrogen-bonding mutations modulate the activity of Amphitrite ornata dehaloperoxidase.

Michael F. Davis, S. Franzen, S. Lommel, 2006, Biochemistry.

Structural Studies of Inhibitor and Substrate Binding in the Hemoglobin Dehaloperoxidase

Michael F. Davis, 2009 .

Conformational dynamics associated with photodissociation of CO from dehaloperoxidase studied using photoacoustic calorimetry.

Michael F. Davis, J. Miksovska, S. Franzen, 2008, Biochemistry.

Determination of separate inhibitor and substrate binding sites in the dehaloperoxidase-hemoglobin from Amphitrite ornata.

Michael F. Davis, B. Bobay, S. Franzen, 2010, Biochemistry.

X-ray structure of the metcyano form of dehaloperoxidase from Amphitrite ornata: evidence for photoreductive dissociation of the iron-cyanide bond.

Michael F. Davis, R. Rose, S. Franzen, 2010, Acta crystallographica. Section D, Biological crystallography.