Michael A. Davis

Dehaloperoxidase-Hemoglobin from Amphitrite ornata Is Primarily a Monomer in Solution

JOURNAL OF PHYSICAL CHEMISTRY B, 115(14), 4266–4272.

Internal Binding of Halogenated Phenols in Dehaloperoxidase-Hemoglobin Inhibits Peroxidase Function

BIOPHYSICAL JOURNAL, 99(5), 1586–1595.

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

Acta Crystallographica. Section D, Biological Crystallography, 66, 770–782.

Different Modes of Binding of Mono-, Di-, and Trihalogenated Phenols to the Hemoglobin Dehaloperoxidase from Amphitrite ornata

BIOCHEMISTRY, 48(10), 2164–2172.

Conformational Dynamics Associated with Photodissociation of CO from Dehaloperoxidase Studied Using Photoacoustic Calorimetry

BIOCHEMISTRY, 47(44), 11510–11517.

Determinants of Substrate Internalization in the Distal Pocket of Dehaloperoxidase Hemoglobin of Amphitrite ornata

BIOCHEMISTRY, 47(49), 12985–12994.

Substrate binding triggers a switch in the iron coordination in dehaloperoxidase from Amphitrite ornata: HYSCORE experiments

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 130(7), 2128-+.

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

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 63, 1094–1101.

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

BIOCHEMISTRY, 45(30), 9085–9094.

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

BIOCHEMISTRY, 44(48), 15637–15644.

A study of the molecular interactions occurring in blends of cellulose esters and phenolic polymers

In T. J. Heinze & W. G. Glasser (Eds.), ACS Symposium Series 688, Cellulose Derivatives (p. 283).