James O Alben | Ohio State University (original) (raw)

Papers by James O Alben

Journal of Biological Chemistry, Jun 1, 1972

dag^{\dag}dagPresent address: Department of Physiological Chemistry, Ohio State Univeristy, College o... more $^{\dag}$Present address: Department of Physiological Chemistry, Ohio State Univeristy, College of Medicine, Columbus, Ohio. 1^{1}1Fed. Proc., 21, 46 (1962).

Communication at the molecular level is the basis for all forms of biological control. This may r... more Communication at the molecular level is the basis for all forms of biological control. This may range from simple dipole interactions that alter a chemical equilibrium to a complex series of interactions that lead to control of electron transport in the cytochrome system in mitochondria. All of these processes can be analyzed into a series of steps, which in turn can be described in terms of simple molecular force fields. Infrared spectroscopy1 has been an excellent tool for the study of molecular interactions in biological molecules, since chemical bonding, and therefore vibrational force constants, are very sensitive to changes in local molecular interactions. Our understanding of cytochrome c oxidase has been greatly enhanced by direct spectroscopic studies, and by comparisons with metal coordination complexes and simpler heme proteins and hemocyanins.

Journal of Theoretical Biology, May 1, 1978

... BARE, GH, ALBEN, JO, BROMBERG, PA, JONES, RT, BRIMHALL, B. PADILLA, F. (1974). J. biol. Chem.... more ... BARE, GH, ALBEN, JO, BROMBERG, PA, JONES, RT, BRIMHALL, B. PADILLA, F. (1974). J. biol. Chem. 249, 773. CHANCE, EM, HESS, B., PLESSER, T. WURSTER, B. (1975). Eur. J. Biochem. 50, 419. 230 RH MATTHEWS AND JO ALDEN CHRISTENSEN, HN (1964). Proc. ...

PubMed, Oct 1, 2008

Context: Ultrasonography is a valuable diagnostic tool in the clinical setting. Yet, medical stud... more Context: Ultrasonography is a valuable diagnostic tool in the clinical setting. Yet, medical students often have minimal familiarity with this technology. Objective: To evaluate the ability of second-year medical students to use ultrasonography for identification of anatomic structures and pathologic conditions. Design: A self-directed approach that reduced facilitator involvement, encouraging learning that mimicked the medical school's problem-based learning pathway program. Methods: Five students were each given 10 hours of instruction in ultrasonographic techniques by three certified ultrasonographers in outpatient and hospital settings. Each student performed 40 hours of organ-specific ultrasonographic scans on another student in 2-hour sessions during 20 weeks. Images were archived for future evaluation and quality rating. Students took a 35-question posttraining examination with 10 contrived case scenarios. Questions were designed to test student knowledge in three categories: anatomic structure, technical skill, and clinical diagnosis. Results: Posttraining examination results, expressed as the percent of correct answers for all five participants by category, were as follows: anatomic structure, 70%; technical skill, 70%; clinical diagnosis, 68%. Evaluations of the archived images, which were graded for proper anatomic identification and image clarity, yielded the following scores indicating "good" or "fair" quality for each anatomic region: abdominal, 80%; pelvic, 63%; cardiac, 73%. Conclusion: Second-year osteopathic medical students can attain a sufficient degree of proficiency in limited ultrasonographic technique.

Biochemistry, Feb 29, 1972

Recent developments in instrumentation and techniques have made possible studies of coordination ... more Recent developments in instrumentation and techniques have made possible studies of coordination of metal-protein complexes in aqueous solution by infrared spectroscopy. Thus early work with carbon monoxide complexes of hemoglobin, as well as preliminary studies with myoglobin (Mb) complexes, have now been quantitated and extended to the temperature-dependent ionicity of N.3-bound to Mb. Titration of Mb with NaNa produces two peaks, one at 2046 cm-l (ionic) and one at 2023 cm-I (covalent). Both

Annals of the New York Academy of Sciences, 1969

Pi-interactions have played an important role in the development of ideas about porphyrin, metall... more Pi-interactions have played an important role in the development of ideas about porphyrin, metalloporphyrin, and hemeprotein systems. In early studies of the isolation, structure and synthesis of porphyrins, "molecular complexes" such as picrates and flavianates were widely used."* The tendency for hemins to associate in solution was also studied in some detail, although it is still not well under-~t o o d ;~'~ and pi-bonding between iron and axial ligands was introduced to describe bonding of several ligands to iron porphyrins and he me protein^.^ Recent experiments have provided evidence for pi-interaction between the central metal ion and axial ligands, between the metal ion and the porphyrin, and between the porphyrin pi-electron system and the solvent and/or protein environment. PI-BONDING BETWEEN T H E METAL ION A N D AXIAL LIGANDS Iron (ZZ) Compounds. The participation of low-spin iron (11) of hemes and hemeproteins (e.g. hemoglobins and myoglobins) in pi-bonding to ligands was proposed for ligands such as oxygen, carbon monoxide, nitric oxide, and alkylisocyanides in both the early Pauling descriptions5 and in the later parallel-to-the *This work was supported by United States Public Health Service Grant HE-06079.

Biochemistry, 1968

The binding of carbon monoxide to hemes has been studied by high-resolution infrared spectros-* F... more The binding of carbon monoxide to hemes has been studied by high-resolution infrared spectros-* From the

Biochemistry, 1969

The infrared stretching frequencies for carbon monoxide (vCJ bound to various hemoglobins and myo... more The infrared stretching frequencies for carbon monoxide (vCJ bound to various hemoglobins and myoglobins have been determined. The identity of v,, was confirmed by spectra of '*C180 and 13C160 derivatives. For human hemoglobins A, F, H, and Chesapeake and sheep hemoglobins A, B, C, and lamb, one narrow CO absorption was found near 1951 cm-l. However, two absorptions of similar area were found for hemoglobin MEmors (c~~~~P~~~~~) , at 1970 and 1950 cm-l, and for hemoglobin Zurich (~y~* / 3 > ' *~~) , at 1958 and 1951 cm-l. Thus substitution for the amino acid at position 63 of the /3 chain (the position of the I n infrared spectra of human carbonyl hemoglobin A, both within or isolated from the red blood cell, a single narrow absorption band at 1951 cm-l was found (Alben and Caughey, 1966, 1968). The assignment of this absorption to the stretching frequency (veJ of carbon monoxide was confirmed by shifts in frequency found with isotopically labeied carbon monoxide. Interpretations of these data included consideration of (1) the frequency, which was consistent with relatively strong bonding between CO and iron, (2) the presence of a single absorption band, which reflected an essentially equal strength of CO binding to each heme iron, and (3) the band width of only 8 cm-l at half-peak height, which was indicative of a rather nonpolar environment. The present report of infrared spectra for H b A and nine other hemoglobins and for two myoglobins considers effects of known changes in protein structure upon CO and O2 binding, as measured by vcO, Some of this work has appeared in preliminary reports (Alben and Caughey, 1966,1968; Caughey et al., 1968).

Elsevier eBooks, 1978

Studies on the effect of chloride on the oxygen equilibrium of a hemoglobin derivative specifical... more Studies on the effect of chloride on the oxygen equilibrium of a hemoglobin derivative specifically carbamylated at Val-1 (β) have indicated that this residue is not a major, oxygen-linked binding site for this anion. The postulate that Lys-82 (β) is a major binding site for chloride is supported by results on mutant hemoglobins from other laboratories. The second major, oxygen-linked binding site for chloride is Val-1 of the α-chain. Studies on a mutant hemoglobin derivative where both Lys-82 (β) and Val-1 (α) are altered indicate that the effect of chloride on the oxygen equilibrium is mediated through these residues to the extent of about 80%.

Journal of Biological Chemistry, Jun 1, 1980

A hemoglobin hybrid in which the a chains have NH2-terminal residues that have been blocked speci... more A hemoglobin hybrid in which the a chains have NH2-terminal residues that have been blocked specifically by carbamylation and / 3 chains that have been derived from hemoglobin Providence I @82 Lys-f Asn) was prepared. This derivative shows a small but significant dependence of its oxygen equilibrium curve on the concentration of chloride, phosphate, or nitrate. These data were compared with oxygen-linked anion binding to hemoglobins A and Providence, and to the carbamylated hybrid, atc&, by fitting equations to the data with the use of MULTIFIT 11, a nonlinear curve-fitting program. Dependence of the anion dissociation constants from deoxygenated (KO) and fully oxygenated (KO) hemoglobins upon the mathematical model is described. The data provide further support that Val-1 (a) and Lys-82 (8) of hemoglobin are major, oxygen-linked binding sites for small inorganic anions and suggest that a third oxygen-linked site may also be present. Organic and inorganic anions are positive heterotropic effectors of oxygen binding to hemoglobin as they have a higher affinity for deoxy compared with the oxy conformation of the protein. 2,3-Diphosphoglyceric acid, the organic anion found within the mammalian erythrocyte (1, 2), binds at a single site between the two p chains of deoxyhemoglobin in a cluster of four positively charged side chains on each , L? subunit (3). Some of these residues have been considered as candidates for the binding site of small inorganic anions. Subsequent studies excluded His-2 (p) (4) and His-143 (p) (6) as binding sites for inorganic anions. After studies on hemoglobin carbamylated specifically at Val-1 (p), we proposed that Lys-82 ' The abbreviations used are: HMB, hydroxymercuribenzoate; bis-Tris, bis(Z-hydroxyethyl)imino-tris(hydroxymethyl)methane.

Biochemistry, Dec 1, 1985

The structures of photoactivated carboxymyoglobin (Mb*CO) at temperatures to 10 K have been inves... more The structures of photoactivated carboxymyoglobin (Mb*CO) at temperatures to 10 K have been investigated by Fourier transform infrared (FT-IR) spectroscopy, visible spectroscopy, and near-infrared spectroscopy. Two energy states for *CO are observed by FT-IR, which are altered in frequency by 94% and 88% of the difference from the ground-state heme CO toward free C O gas [Alben, J.

Springer eBooks, 1988

Cytochrome c oxidase is the terminal enzyme in electron transport. It catalyzes the transfer of f... more Cytochrome c oxidase is the terminal enzyme in electron transport. It catalyzes the transfer of four electrons from cytochrome c and four protons of unknown origin to dioxygen, which is converted into two molecules of water. (For a thorough review see Wikstrom et al., 1981). Mammalian cytochrome oxidase is a large Y-shaped molecule that spans the inner mitochondrial membrane (Deatherage et al., 1983; Kim et al., 1985), and consists of one copy of each of 1–13 subunits (Kadenbach et al., 1986; Kuhn-Nentwig and Kadenbach, 1985 & 1986; Buse et al., 1985; Capaldi and Zhang, 1986). The enzyme has two functional domains: cytochrome a, which contains one heme (aFe) and one copper (CuA); and cytochrome a3, which contains the remaining herae (a3Fe) and copper (CuB). Cytochrome a3 is the site of ligand binding and dioxygen reduction.

Proceedings of SPIE, Jan 31, 1994

The need to extract spectral information from biological samples has led to the use of photopertu... more The need to extract spectral information from biological samples has led to the use of photoperturbation spectroscopy at cryogenic temperatures, which selectively extracts only those vibrational modes that are perturbed. When the desired bands are overlapped by strong solvent absorptions, ultrathin transmission paths must be used. The desired bands must then be distinguished from atmospheric absorptions, phase errors, and instrumental non-linearities. Applications to biological problems are presented.

Biochemistry, May 1, 1990

Ethanol has been observed to cause a perturbation of the catalytic center of the major respirator... more Ethanol has been observed to cause a perturbation of the catalytic center of the major respiratory protein cytochrome c oxidase. These effects were examined by Fourier transform infrared spectroscopy of carbon monoxide complexes of cytochrome a3Fe and of Cue formed by low-temperature photodissociation of the a 3 F e C 0 complex. Carbon monoxide binds to reduced cytochrome oxidase in two major structural forms, a and p, both of which are altered by ethanol. In the absence of ethanol, 15-2296 of the total cytochrome oxidase in beef heart mitochondria was observed as P-forms. Ethanol addition caused a concentration-dependent elimination of the @forms with 40% disappearing at 0.05 M (0.23%) ethanol, a concentration that can readily be achieved in the blood of intoxicated individuals. At 0.5 M (2.3%) ethanol and above, almost no p-forms were detectable. The C U-C U~C O absorption normally splits into two bands at temperatures below 40 K. This effect was decreased in the presence of ethanol and eliminated by high ethanol concentrations. It appears that ethanol increases the structural fluctuations at the active site of the enzyme, analogous to the effects of increased temperature. There was an 8-10% decrease in the maximum rate of oxygen reduction by mitochondrial cytochrome oxidase in 0.05 M ethanol at 24 O C , while higher concentrations of ethanol caused no further inhibition. This is the first demonstration that aand /3-forms of cytochrome c oxidase can be modified by an externally added reagent. Changes in the spectra of a-CuBC0 in the presence of 50% (v/v) ethylene glycol were quite striking, but variable. In contrast, the effect of glycerol appears to be limited to extraction of water, as samples prepared with glycerol had spectra similar to those of aqueous preparations. Low-temperature splitting of the C U-C U~C O band is consistent with an exchange process due to H-bond formation between an ionizable ligand to a-CuB and an adjacent ionizable group from the protein. Ethanol disrupts this interaction. A model is presented. We suggest that these data require the presence of a mobile proton adjacent to the coordinated Cue complex. Such a proton may participate in dioxygen reduction to water or in proton pumping mechanisms. A corresponding exchange process is not observed in P-forms of cytochrome c oxidase. E have previously shown that heart mitochondrial cytochrome c oxidase can exist in several structures that are defined as a-and multiple @-forms (Alben et al., 1981; Fiamingo et al., 1982) and that the relative amounts of these structural forms depend upon the preparation (Fiamingo et al., 1986, 1988). With the use of Fourier transform infrared spectroscopy of the reduced enzyme exposed to carbon monoxide, these structural forms can be described and quantitatively distinguished by the absorption characteristics of the CO bound at the a3Fe-CuB catalytic site. Photodissociation of a3FeC0 produces a CuBCO complex that is stable below 140 K but dissociates to reform the a3FeC0 complex at higher temperatures. We have observed two types of cytochrome oxidase a3FeC0 structures: an a-form, characterized by a narrow absorption band (2.4-3.2-cm-' bandwidth) centered at 1963 cm-' and observed in every sample studied, and several @-forms 'This study has been supported in part by Grants 87-12A and 87-12C from the Central Ohio Heart Chapter of the American Heart Association (to F.G.F.), by Grants HL-28144 and RR-01739 (to J.O.A.

Journal of Biological Chemistry, Feb 1, 1974

... AND FERNANDO PADILLA From the Departments of Physiological Chemistry and Medicine, Ohio State... more ... AND FERNANDO PADILLA From the Departments of Physiological Chemistry and Medicine, Ohio State University College of Medicine, Columbus, Ohio 43210; the Department of Biochemistry, University of Oregon Medical School, Portland, Oregon 97201; and the Little Rock ...

Nature, 1976

STUDIES of abnormal human haemoglobins (Hbs) with increased O2 affinity have been particularly us... more STUDIES of abnormal human haemoglobins (Hbs) with increased O2 affinity have been particularly useful in developing detailed molecular interpretations of normal Hb function. A number of functionally interesting mutants are altered in the βHC region but only one variant, Hb Hiroshima (β146 His→Asp)1,2, has been reported as having a substitution at the C terminus itself. We report here the structure and O2 equilibria of Hb York, a new mutation at the β146 position, His→Pro, associated with increased O2 affinity, decreased cooperativity and diminished Bohr effect.