Dr. William Henry Woodruff DDS
Dentist
6280 Orchard Lake Rd West Bloomfield MI, 48322About
Dr. William Woodruff is a Dentist practicing in West Bloomfield, MI. Dr. Woodruff specializes in preventing, diagnosing, and treating diseases and conditions associated with the mouth and overall dental health. Dentists are trained to carry out such treatment as professional cleaning, restorative, prosthodontic, and endodontic procedures, and performing examinations, among many others.
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Expert Publications
Data provided by the National Library of Medicine- Assignment of the heme axial ligand(s) for the ferric myoglobin (H93G) and heme oxygenase (H25A) cavity mutants as oxygen donors using magnetic circular dichroism.
- Native azurin and its Ni(II) derivative: a resonance Raman study.
- Native azurin and its Ni(II) derivative: a resonance Raman study.
- A photolysis-triggered heme ligand switch in H93G myoglobin.
- Resonance Raman spectra of cobalt myoglobins and cobalt porphyrins. Evaluation of protein effects on porphyrin structure.
- Time-resolved step-scan Fourier transform infrared spectroscopy of the CO adducts of bovine cytochrome c oxidase and of cytochrome bo(3) from Escherichia coli.
- Allometric scaling of metabolic rate from molecules and mitochondria to cells and mammals.
- Direct infrared detection of the covalently ring linked His-Tyr structure in the active site of the heme-copper oxidases.
- Physiology: Why does metabolic rate scale with body size?
- Resonance Raman studies of Rieske-type proteins.
- Reaction of cyanide with cytochrome ba3 from Thermus thermophilus: spectroscopic characterization of the Fe(II)a3-CN.Cu(II)B-CN complex suggests four 14N atoms are coordinated to CuB.
- Ultrafast infrared spectroscopy.
- An EPR, ESEEM, structural NMR, and DFT study of a synthetic model for the covalently ring-linked tyrosine-histidine structure in the heme-copper oxidases.
- FTIR studies of internal proton transfer reactions linked to inter-heme electron transfer in bovine cytochrome c oxidase.
- The metabolic basis of whole-organism RNA and phosphorus content.
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