Physician
Internal Medicine
Dr. Thomas Spiro, MD
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Thomas Spiro, MD is an expert in the field of Internal Medicine. He researched medicine at Saint Louis University School of Medicine. Saint Louis University School of Medicine has a rank of 67 in research and a 57 in primary care He over the years received 1 awards: "CMS Meaningful Use Stage 1 Certification". Doctor Thomas Spiro, MD is also a published MD. He has 101 paper published. The most recent paper is: Picosecond resonance Raman evidence for unrelaxed heme in the (carbonmonoxy)myoglobin photoproduct. Dr. Thomas Spiro is registered with Medicare and accepts Medicare payments.
Publications
- Differential Control of Heme Reactivity in Alpha and Beta Subunits of Hemoglobin: A Combined Raman Spectroscopic and Computational Study.
- Ultrafast charge transfer in nickel phthalocyanine probed by femtosecond Raman-induced kerr effect spectroscopy.
- Distinguishing unfolding and functional conformational transitions of calmodulin using ultraviolet resonance Raman spectroscopy.
- Mn(II,III) oxidation and MnO2 mineralization by an expressed bacterial multicopper oxidase.
- CO, NO and O2 as Vibrational Probes of Heme Protein Interactions.
- Is the CO adduct of myoglobin bent, and does it matter?
- Cobalt II substitution in the type 1 site of the multi-copper oxidase Rhus laccase.
- Absence of heme-localized strain in T state hemoglobin: insensitivity of heme-imidazole resonance Raman frequencies to quaternary structure.
- Substrate polarization by residues in delta 5-3-ketosteroid isomerase probed by site-directed mutagenesis and UV resonance Raman spectroscopy.
- Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: resonance Raman evidence from Leu-52 and Gly-181 mutants of cytochrome c pero...
- Resonance Raman spectroscopy of cytochrome c peroxidase single crystals on a variable-temperature microscope stage.
- Resonance Raman evidence for low-spin Fe2+ heme a3 in energized cytochrome c oxidase: implications for the inhibition of O2 reduction.
- Probing protein structure and dynamics with resonance Raman spectroscopy: cytochrome c peroxidase and hemoglobin.
- Single-crystal resonance Raman spectroscopy of site-directed mutants of cytochrome c peroxidase.
- Resonance Raman evidence that distal histidine protonation removes the steric hindrance to upright binding of carbon monoxide by myoglobin.
- Ionic strength dependence of cytochrome c structure and Trp-59 H/D exchange from ultraviolet resonance Raman spectroscopy.
- Photodissociable endogenous ligand in alkaline-reduced cytochrome c peroxidase implicates distal protein tension.
- Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes.
- Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes.
- Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 3. Bound ligand vibrational modes.
- Ultraviolet resonance Raman spectroscopy of distamycin complexes with poly(dA)-poly(dT) and poly(dA-dT): role of H-bonding.
- Heme pocket interactions in cytochrome c peroxidase studied by site-directed mutagenesis and resonance Raman spectroscopy.
- Cytochrome c peroxidase mutant active site structures probed by resonance Raman and infrared signatures of the CO adducts.
- Resonance Raman spectroscopy and enhanced photoreducibility for the 420 nm pulsed form of cytochrome oxidase.
- Resonance Raman spectroscopy shows different temperature-dependent coordination equilibria for native horseradish and cytochrome c peroxidase.
- Resonance Raman spectra of the pyridoxal coenzyme in aspartate aminotransferase. Evidence for pyridine protonation and a novel photochemical H/D exchange at the imine ...
- Resonance Raman spectroscopy as a probe of heme protein structure and dynamics.
- Ultraviolet resonance Raman spectra of cytochrome c conformational states.
- Resonance Raman evidence for an exchangeable protein hydrogen associated with the heme a group of cytochrome oxidase.
- Transient resonance Raman spectroscopy shows unrelaxed heme following CO photodissociation from cytochrome-c peroxidase.
- Raman and infrared spectra of cytochrome c peroxidase-carbon monoxide adducts in alternative conformational states.
- An investigation of hydrogenase I and hydrogenase II from Clostridium pasteurianum by resonance Raman spectroscopy. Evidence for a [2Fe-2S] cluster in hydrogenase I.
- Tyrosine and tryptophan modification monitored by ultraviolet resonance Raman spectroscopy.
- Tyrosine hydrogen-bonding and environmental effects in proteins probed by ultraviolet resonance Raman spectroscopy.
- Ultraviolet resonance Raman spectroscopy as a probe of protein structure in the fd virus.
- 63/65Cu and 1/2H2O isotope shifts in the low-temperature resonance Raman spectrum of fungal laccase.
- Secondary structure determination in proteins from deep (192-223-nm) ultraviolet Raman spectroscopy.
- Resonance Raman spectroscopic evidence that carp deoxyhemoglobin remains in a T-like quaternary structure at high pH: implications for cooperativity.
- Ultraviolet Raman spectroscopy indicates fast (less than 7 ns) R----T-like motion in hemoglobin.
- Alternative carbon monoxide binding modes for horseradish peroxidase studied by resonance Raman spectroscopy.
- Resonance Raman characterization of the 7-ns photoproduct of (carbonmonoxy)hemoglobin: implications for hemoglobin dynamics.
- Ultraviolet resonance Raman spectra of insulin and alpha-lactalbumin with 218- and 200-nm laser excitation.
- Nanosecond transient resonance Raman spectra of the FeII-CO and FeIII-NO photolysis products of horseradish peroxidase.
- Raman spectroscopic elucidation of DNA backbone conformations for poly(dG-dT).poly(dA-dC) and poly(dA-dT).poly(dA-dT) in CsF solution.
- Resonance Raman spectroscopy of pyridoxal Schiff bases.
- Picosecond resonance Raman evidence for unrelaxed heme in the (carbonmonoxy)myoglobin photoproduct.
- A twist on heme signaling.
- Phase I clinical and pharmacokinetic study of rebeccamycin analog NSC 655649 given daily for five consecutive days.
- Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/Vis absorption s...
- UV Raman monitoring of histidine protonation and H-(2)H exchange in plastocyanin.
- Activation of soluble guanylyl cyclase by four-coordinate metalloporphyrins: evidence for a role for porphyrin conformation.
- Comparison and contrasts between the active site PKs of Mn-superoxide dismutase and those of Fe-superoxide dismutase.
- Site mutations disrupt inter-helical H-bonds (alpha14W-alpha67T and beta15W-beta72S) involved in kinetic steps in the hemoglobin R-->T transition without altering the ...
- FeNO structure in distal pocket mutants of myoglobin based on resonance Raman spectroscopy.
- Activation mechanism of the CO sensor CooA. Mutational and resonance Raman spectroscopic studies.
- Vibrational and electronic couplings in ultraviolet resonance Raman spectra of cyclic peptides.
- Role of ligand bending in the photodissociation of O2 vs CO-heme: a time-dependent density functional study.
- Dynamics of carbon monoxide binding to CooA.
- Time-resolved absorption and UV resonance Raman spectra reveal stepwise formation of T quaternary contacts in the allosteric pathway of hemoglobin.
- Hemoglobin site-mutants reveal dynamical role of interhelical H-bonds in the allosteric pathway: time-resolved UV resonance Raman evidence for intra-dimer coupling.
- CO as a vibrational probe of heme protein active sites.
- Porphyrin distortion during affinity maturation of a ferrochelatase antibody, monitored by Resonance Raman spectroscopy.
- Tunable kHz deep ultraviolet (193-210 nm) laser for Raman application.
- Early events in apomyoglobin unfolding probed by laser T-jump/UV resonance Raman spectroscopy.
- Spectroscopic studies of the anaerobic enzyme-substrate complex of catechol 1,2-dioxygenase.
- Dynamics of allostery in hemoglobin: roles of the penultimate tyrosine H bonds.
- Intermediacy of poly(L-proline) II and beta-strand conformations in poly(L-lysine) beta-sheet formation probed by temperature-jump/UV resonance Raman spectroscopy.
- Pulling NO out of thin air.
- Dynamics of carbon monoxide binding to cystathionine beta-synthase.
- Spectroscopic studies of the corrinoid/iron-sulfur protein from Moorella thermoacetica.
- Temperature-jump apparatus with Raman detection based on a solid-state tunable (1.80-2.05 microm) kHz optical parametric oscillator laser.
- Modeling of ligation-induced helix/loop displacements in myoglobin: toward an understanding of hemoglobin allostery.
- DFT analysis of co-alkyl and co-adenosyl vibrational modes in B12-cofactors.
- Porphyrin distortion from resonance Raman intensities of out-of-plane modes: Computation and modeling of N-methylmesoporphyrin, a ferrochelatase transition state analog.
- Quantum chemical evaluation of protein control over heme ligation: CO/O2 discrimination in myoglobin.
- Heme displacement mechanism of CooA activation: mutational and Raman spectroscopic evidence.
- Microsecond melting of a folding intermediate in a coiled-coil peptide, monitored by T-jump/UV Raman spectroscopy.
- Differential sensing of protein influences by NO and CO vibrations in heme adducts.
- A conformational switch to beta-sheet structure in cytochrome c leads to heme exposure. Implications for cardiolipin peroxidation and apoptosis.
- Density functional theory analysis of molybdenum isotope fractionation.
- Mechanism of the CO-sensing heme protein CooA: new insights from the truncated heme domain and UVRR spectroscopy.
- Trans-dioxo manganese(V) porphyrins.
- Enthalpic and entropic stages in alpha-helical peptide unfolding, from laser T-jump/UV Raman spectroscopy.
- Adventures in bioinorganic chemistry.
- Cu(I) recognition via cation-pi and methionine interactions in CusF.
- DFT analysis of axial and equatorial effects on heme-CO vibrational modes: applications to CooA and H-NOX heme sensor proteins.
- Characterization of two different five-coordinate soluble guanylate cyclase ferrous-nitrosyl complexes.
- Protein dynamics from time resolved UV Raman spectroscopy.
- Modulation of the heme electronic structure and cystathionine beta-synthase activity by second coordination sphere ligands: The role of heme ligand switching in redox ...
- Subunit-selective interrogation of CO recombination in carbonmonoxy hemoglobin by isotope-edited time-resolved resonance Raman spectroscopy.
- Linking conformation change to hemoglobin activation via chain-selective time-resolved resonance Raman spectroscopy of protoheme/mesoheme hybrids.
- Heme regulation of human cystathionine beta-synthase activity: insights from fluorescence and Raman spectroscopy.
- Bacteriogenic manganese oxides.
- New light on NO bonding in Fe(III) heme proteins from resonance Raman spectroscopy and DFT modeling.
- Probing soluble guanylate cyclase activation by CO and YC-1 using resonance Raman spectroscopy.
- Soluble guanylate cyclase is activated differently by excess NO and by YC-1: resonance Raman spectroscopic evidence.
- Quaternary speeding in hemoglobin.
- Probing domain interactions in soluble guanylate cyclase.
- Reversible heme-dependent regulation of human cystathionine ?-synthase by a flavoprotein oxidoreductase.
- Heme Reactivity is Uncoupled from Quaternary Structure in Gel-Encapsulated Hemoglobin: A Resonance Raman Spectroscopic Study.
Schools
Saint Louis University School Of Medicine
St Marys Health Center
Doctors Specialties
- Internal Medicine
Accepted Insurances
Awards
- CMS Meaningful Use Stage 1 Certification
Education
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Saint Louis University School of Medicine
Drug Facts
| NPI NUMBER | 1215955455 | |
| NPPES Provider LastName | SPIRO | |
| NPPES Provider FirstName | THOMAS | |
| NPPES Provider ZIPCode | 631171854 | |
| NPPES Provider State | MO | |
| Specialty Description | Internal Medicine | |
| Total Claim Count | 7521.0 | |
| Distinct Opioid Count | 8.0 | |
| Opioid Claim Count | 414.0 | |
| Percent Opioid Claims | 5.5 |
Helpful Reviews
Medicare Facts
| National Provider Identifier [NPI] | 1215955455 |
| Last Name Of The Provider | SPIRO |
| First Name Of The Provider | THOMAS |
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