James T. Hazzard

2.1k total citations
46 papers, 1.8k citations indexed

About

James T. Hazzard is a scholar working on Molecular Biology, Electrical and Electronic Engineering and Physical and Theoretical Chemistry. According to data from OpenAlex, James T. Hazzard has authored 46 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 15 papers in Electrical and Electronic Engineering and 9 papers in Physical and Theoretical Chemistry. Recurrent topics in James T. Hazzard's work include Photosynthetic Processes and Mechanisms (25 papers), Electrochemical sensors and biosensors (11 papers) and Electrochemical Analysis and Applications (9 papers). James T. Hazzard is often cited by papers focused on Photosynthetic Processes and Mechanisms (25 papers), Electrochemical sensors and biosensors (11 papers) and Electrochemical Analysis and Applications (9 papers). James T. Hazzard collaborates with scholars based in United States, Canada and Italy. James T. Hazzard's co-authors include Gordon Tollin, John H. Enemark, T.L. Poulos, Changjian Feng, Michael A. Cusanovich, John K. Hurley, W.R. Montfort, A. Weichsel, Gregor Grass and Sue A. Roberts and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

James T. Hazzard

46 papers receiving 1.8k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name	h						Papers	Cites
James T. Hazzard United States	27	1.1k	428	361	313	278	46	1.8k
Angel J. Di Bilio United States	28	1.2k 1.1×	423 1.0×	433 1.2×	692 2.2×	257 0.9×	45	2.8k
Takamitsu Kohzuma Japan	24	903 0.8×	174 0.4×	372 1.0×	561 1.8×	133 0.5×	95	1.7k
Michael H. Klapper United States	24	1.1k 1.0×	249 0.6×	85 0.2×	201 0.6×	197 0.7×	66	2.1k
Raymond E. Hansen United States	23	1.1k 1.0×	189 0.4×	286 0.8×	156 0.5×	164 0.6×	37	1.7k
Mei M. Whittaker United States	33	1.4k 1.3×	154 0.4×	470 1.3×	1.8k 5.7×	134 0.5×	55	3.3k
Marcel Asso France	24	655 0.6×	184 0.4×	780 2.2×	414 1.3×	103 0.4×	57	1.6k
Parisa Hosseinzadeh United States	20	956 0.9×	218 0.5×	422 1.2×	453 1.4×	117 0.4×	36	1.8k
M. Faraggi Israel	22	638 0.6×	143 0.3×	95 0.3×	341 1.1×	146 0.5×	62	1.5k
Chantal Houée‐Levin France	28	975 0.9×	78 0.2×	127 0.4×	374 1.2×	74 0.3×	127	2.2k
Harold M. Goff United States	29	858 0.8×	230 0.5×	127 0.4×	861 2.8×	155 0.6×	105	2.5k

Countries citing papers authored by James T. Hazzard

Since Specialization

Citations

This map shows the geographic impact of James T. Hazzard's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by James T. Hazzard with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites James T. Hazzard more than expected).

Fields of papers citing papers by James T. Hazzard

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by James T. Hazzard. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by James T. Hazzard. The network helps show where James T. Hazzard may publish in the future.

Co-authorship network of co-authors of James T. Hazzard

This figure shows the co-authorship network connecting the top 25 collaborators of James T. Hazzard. A scholar is included among the top collaborators of James T. Hazzard based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with James T. Hazzard. James T. Hazzard is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Feng, Changjian, Linda J. Roman, James T. Hazzard, et al.. (2008). Deletion of the autoregulatory insert modulates intraprotein electron transfer in rat neuronal nitric oxide synthase. FEBS Letters. 582(18). 2768–2772. 29 indexed citations

Roberts, Sue A., A. Weichsel, Gregor Grass, et al.. (2002). Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli. Proceedings of the National Academy of Sciences. 99(5). 2766–2771. 276 indexed citations

Hurley, John K., James T. Hazzard, Marta Martínez‐Júlvez, et al.. (1999). Electrostatic forces involved in orienting Anabaena ferredoxin during binding to Anabaena ferredoxin:NAdp⁺ reductase: Site‐specific mutagenesis, transient kinetic measurements, and electrostatic surface potentials. Protein Science. 8(8). 1614–1622. 43 indexed citations

Pacheco, A. Andrew, James T. Hazzard, Gordon Tollin, & John H. Enemark. (1999). The pH dependence of intramolecular electron transfer rates in sulfite oxidase at high and low anion concentrations. JBIC Journal of Biological Inorganic Chemistry. 4(4). 390–401. 82 indexed citations

Hazzard, James T., Shanthi Govindaraj, T.L. Poulos, & Gordon Tollin. (1997). Electron Transfer between the FMN and Heme Domains of Cytochrome P450BM-3. Journal of Biological Chemistry. 272(12). 7922–7926. 36 indexed citations

Hazzard, James T., et al.. (1997). Laser Flash Photolysis Experiments on the Effects of Freezing and Salt Addition on Intramolecular Electron Transfer within One-Electron Reduced Ascorbate Oxidase. Archives of Biochemistry and Biophysics. 339(1). 24–32. 6 indexed citations

Hazzard, James T., A. MARCHESINI, P. Curir, & Gordon Tollin. (1994). Direct measurement by laser flash photolysis of intramolecular electron transfer in the three-electron reduced form of ascorbate oxidase from zucchini. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1208(1). 166–170. 14 indexed citations

Hazzard, James T., et al.. (1994). Intramolecular Electron Transfer in Yeast Flavocytochrome b2 upon One-Electron Photooxidation of the Fully Reduced Enzyme: Evidence for Redox State Control of Heme-Flavin Communication. Biochemistry. 33(45). 13445–13454. 11 indexed citations

Hazzard, James T., et al.. (1992). Inhibition of intramolecular electron transfer in sulfite oxidase by anion binding. Journal of the American Chemical Society. 114(24). 9662–9663. 26 indexed citations

10.

Hazzard, James T., A. Grant Mauk, & Gordon Tollin. (1992). Laser flash photolysis studies of electron transfer mechanisms in cytochromes: An aromatic residue at position 82 is not required for cytochrome c reduction by flavin semiquinones or electron transfer from cytochrome c to cytochrome oxidase. Archives of Biochemistry and Biophysics. 298(1). 91–95. 12 indexed citations

11.

Hazzard, James T., et al.. (1991). Unimolecular and bimolecular oxidoreduction reactions involving diprotein complexes of cytochrome c and plastocyanin. Dependence of electron-transfer reactivity on charge and orientation of the docked metalloproteins. Biochemistry. 30(38). 9297–9304. 38 indexed citations

12.

Tollin, Gordon & James T. Hazzard. (1991). Intra- and intermolecular electron transfer processes in redox proteins. Archives of Biochemistry and Biophysics. 287(1). 1–7. 47 indexed citations

13.

Walker, Mark C., James T. Hazzard, Gordon Tollin, & Dale E. Edmondson. (1991). Kinetic comparison of reduction and intramolecular electron transfer in milk xanthine oxidase and chicken liver xanthine dehydrogenase by laser flash photolysis. Biochemistry. 30(24). 5912–5917. 14 indexed citations

14.

Hazzard, James T., William S. McIntire, & Gordon Tollin. (1991). Laser flash photolysis study of intermolecular and intramolecular electron transfer in trimethylamine dehydrogenase. Biochemistry. 30(18). 4559–4564. 5 indexed citations

15.

Hazzard, James T., Susan J. Moench, James E. Erman, James D. Satterlee, & Gordon Tollin. (1988). Kinetics of intracomplex electron transfer and of reduction of the components of covalent and noncovalent complexes of cytochrome c and cytochrome c peroxidase by free flavin semiquinones. Biochemistry. 27(6). 2002–2008. 44 indexed citations

16.

Hazzard, James T., George McLendon, Michael A. Cusanovich, & Gordon Tollin. (1988). Formation of electrostatically-stabilized complex at low ionic strength inhibits interprotein electron transfer between yeast cytochrome c and cytochrome c peroxidase. Biochemical and Biophysical Research Communications. 151(1). 429–434. 45 indexed citations

17.

Mauro, J. Matthew, Laurence A. Fishel, James T. Hazzard, et al.. (1988). Tryptophan-191 .fwdarw. phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation. Biochemistry. 27(17). 6243–6256. 121 indexed citations

18.

Eltis, Lindsay D., A. Grant Mauk, James T. Hazzard, M. A. Cusanovich, & Gordon Tollin. (1988). Kinetics of flavin semiquinone reduction of the components of the cytochrome c-cytochrome b5 complex. Biochemistry. 27(15). 5455–5460. 11 indexed citations

19.

Hazzard, James T., T.L. Poulos, & Gordon Tollin. (1987). Kinetics of reduction by free flavin semiquinones of the components of the cytochrome c-cytochrome c peroxidase complex and intracomplex electron transfer. Biochemistry. 26(10). 2836–2848. 58 indexed citations

20.

Hazzard, James T. & Gordon Tollin. (1985). Proton NMR study of the cytochrome c: Flavodoxin electron transfer complex. Biochemical and Biophysical Research Communications. 130(3). 1281–1286. 13 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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