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Israel Hanukoglu
Israel Hanukoglu (Turkish: İsrael Hanukoğlu, Hebrew: ישראל חנוכוגלו) is a Turkish-born Israeli scientist. He is a full professor of biochemistry and molecular biology at Ariel University and former science and technology adviser to the prime minister of Israel (1996–1999). He is founder of Israel Science and Technology Directory.
Israel Hanukoglu attended tr:Şişli Terakki Lisesi in Istanbul until the end of junior high school. In ninth grade, he switched to Atatürk Erkek Lisesi in Taksim, Istanbul, graduating in 1969. In his senior year, he was selected for an American Field Service (AFS) International Scholarship. As an AFS student, he attended Joseph A. Craig High School in Janesville, Wisconsin, and received his high-school diploma in 1970.
Israel Hanukoglu received his undergraduate degree cum laude with double majors in biology and psychology and a minor in political science from the Hebrew University of Jerusalem. He then went to the University of Wisconsin–Madison for graduate studies and received his M.Sc. degree in 1976 in an inter-disciplinary Endocrinology-Reproductive physiology program, under the joint supervision of Prof. Harry J. Karavolas (Dept. of Physiological Chemistry) and Prof. Robert W. Goy (Dept. of Psychology). His Ph.D. thesis research on the "Mechanism of electron transport to cytochrome P-450 in adrenal cortex mitochondrial steroid monooxygenase systems" was carried out under the supervision of Prof. Colin R. Jefcoate. He received his Ph.D. diploma in August 1980.
Prof. Hanukoglu's scientific work concentrated in three different areas outlined below.
Hanukoglu's career in molecular biology started at the Department of Biochemistry of the University of Chicago (1980–1983 with Elaine Fuchs), where he cloned and sequenced cDNAs coding for cytoskeletal proteins, actin and alpha keratins. He elucidated the first structures of cytoskeletal keratin families, and predicted the long helical domains of these proteins. By computerized analysis of amino acid sequences he predicted that the central rod domain of intermediate filament proteins is composed of four helical segments separated by three short linker sequences. Later crystallographic studies have confirmed this as a general model for intermediate filament protein structure.
During his Ph.D. thesis research, Israel isolated the mitochondrial enzymes that catalyze the first step in the synthesis of steroid hormones in all steroidogenic tissues, including the adrenal cortex, and the reproductive organs. The first step of steroidogenesis is dependent on the transfer of electrons from NADPH to a P450 type enzyme (P450scc) via an electron-transfer chain that includes two additional proteins. These proteins are located on the inner mitochondrial membrane. Israel reconstituted this system using proteins he purified, characterized the process of electron transfer between the proteins, and built a kinetic model that simulated precisely the dynamic behavior of this complex system.
In his first academic position at the Department of Biology at the Technion-Israel Institute of Technology, he first determined the molar stoichiometry of the mitochondrial P450 system proteins using specific antibodies that he generated. He then set out to clone the cDNAs and the genes that code for these enzymes. His lab was the first to clone the cDNAs and the gene coding for adrenodoxin reductase - the first enzyme in the electron transfer chain of the mitochondrial P450 system.
By sequence and structural analyses of adrenodoxin reductase, Israel identified its binding sites for the electron donor and acceptor coenzymes, NADPH and FAD. By sequence analyses of the large oxidoreductase type of enzyme families, he noted that the FAD-binding site is a classical Rossmann fold, but the NADPH binding site has a different consensus sequence that could be responsible for NAD vs. NADP coenzyme specificity. The importance of the motifs he identified was confirmed by re-engineering of coenzyme specificities of different enzymes. Elucidation of the crystal structure of adrenodoxin reductase further verified Israel's identification of the coenzyme binding sites. Analysis of the phylogeny of this enzyme in eukaryotes showed that the NADP binding site sequence is strictly conserved.
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Israel Hanukoglu
Israel Hanukoglu (Turkish: İsrael Hanukoğlu, Hebrew: ישראל חנוכוגלו) is a Turkish-born Israeli scientist. He is a full professor of biochemistry and molecular biology at Ariel University and former science and technology adviser to the prime minister of Israel (1996–1999). He is founder of Israel Science and Technology Directory.
Israel Hanukoglu attended tr:Şişli Terakki Lisesi in Istanbul until the end of junior high school. In ninth grade, he switched to Atatürk Erkek Lisesi in Taksim, Istanbul, graduating in 1969. In his senior year, he was selected for an American Field Service (AFS) International Scholarship. As an AFS student, he attended Joseph A. Craig High School in Janesville, Wisconsin, and received his high-school diploma in 1970.
Israel Hanukoglu received his undergraduate degree cum laude with double majors in biology and psychology and a minor in political science from the Hebrew University of Jerusalem. He then went to the University of Wisconsin–Madison for graduate studies and received his M.Sc. degree in 1976 in an inter-disciplinary Endocrinology-Reproductive physiology program, under the joint supervision of Prof. Harry J. Karavolas (Dept. of Physiological Chemistry) and Prof. Robert W. Goy (Dept. of Psychology). His Ph.D. thesis research on the "Mechanism of electron transport to cytochrome P-450 in adrenal cortex mitochondrial steroid monooxygenase systems" was carried out under the supervision of Prof. Colin R. Jefcoate. He received his Ph.D. diploma in August 1980.
Prof. Hanukoglu's scientific work concentrated in three different areas outlined below.
Hanukoglu's career in molecular biology started at the Department of Biochemistry of the University of Chicago (1980–1983 with Elaine Fuchs), where he cloned and sequenced cDNAs coding for cytoskeletal proteins, actin and alpha keratins. He elucidated the first structures of cytoskeletal keratin families, and predicted the long helical domains of these proteins. By computerized analysis of amino acid sequences he predicted that the central rod domain of intermediate filament proteins is composed of four helical segments separated by three short linker sequences. Later crystallographic studies have confirmed this as a general model for intermediate filament protein structure.
During his Ph.D. thesis research, Israel isolated the mitochondrial enzymes that catalyze the first step in the synthesis of steroid hormones in all steroidogenic tissues, including the adrenal cortex, and the reproductive organs. The first step of steroidogenesis is dependent on the transfer of electrons from NADPH to a P450 type enzyme (P450scc) via an electron-transfer chain that includes two additional proteins. These proteins are located on the inner mitochondrial membrane. Israel reconstituted this system using proteins he purified, characterized the process of electron transfer between the proteins, and built a kinetic model that simulated precisely the dynamic behavior of this complex system.
In his first academic position at the Department of Biology at the Technion-Israel Institute of Technology, he first determined the molar stoichiometry of the mitochondrial P450 system proteins using specific antibodies that he generated. He then set out to clone the cDNAs and the genes that code for these enzymes. His lab was the first to clone the cDNAs and the gene coding for adrenodoxin reductase - the first enzyme in the electron transfer chain of the mitochondrial P450 system.
By sequence and structural analyses of adrenodoxin reductase, Israel identified its binding sites for the electron donor and acceptor coenzymes, NADPH and FAD. By sequence analyses of the large oxidoreductase type of enzyme families, he noted that the FAD-binding site is a classical Rossmann fold, but the NADPH binding site has a different consensus sequence that could be responsible for NAD vs. NADP coenzyme specificity. The importance of the motifs he identified was confirmed by re-engineering of coenzyme specificities of different enzymes. Elucidation of the crystal structure of adrenodoxin reductase further verified Israel's identification of the coenzyme binding sites. Analysis of the phylogeny of this enzyme in eukaryotes showed that the NADP binding site sequence is strictly conserved.