He was born in the Bronx, New York City, where he spent his childhood. He is one of 3 children, having a younger sister Carol and an older brother Arthur,[1][2] also a biochemist. He obtained his high school diploma from the Bronx High School of Science and a B.S. degree, majoring in chemistry, from the City College of New York (1953).
Upon graduation, he was recruited by Dr. Sidney Udenfriend to the National Heart Institute of National Institutes of Health (NIH) to enter a new joint graduate program between the NIH and George Washington University. He received his Ph.D. from George Washington University (Thesis: Studies on 5-Hydroxyindole Metabolism, 1957) based on research done at the NIH in the Udenfriend laboratory. In 1958 the NIH supported his postdoctoral studies done with Dr. H.A. Barker[3] at the University of California at Berkeley, where he was involved in the discovery of the coenzyme form of vitamin B12.[4][5]
In 1959 he returned to the NIH as an independent investigator where he continued his studies on the role of vitamin B12 in methionine biosynthesis, research that helped to elucidate the known inter-relationship among vitamin 12, folic acid and one carbon metabolism.[6][7] The studies on methionine synthesis led to his collaboration with the Nirenberg laboratory at the NIH shortly after the genetic code was cracked.[8]
By 1967 the Weissbach laboratory was deeply involved in protein synthesis (translation) [9][10][11][12] at which time he accepted a position as associate director of the RIMB to help found the Roche Institute of Molecular Biology (RIMB) with Sidney Udenfriend, and in 1983 he became director of the RIMB and a vice-president of research at Hoffmann-La Roche, Nutley, NJ. The RIMB was involved in the very early days of the emergence of the biotechnology industry and was instrumental in helping Hoffmann-La Roche enter this field.[13] Weissbach described this period at Roche in a book he co-authored with David Fisher in 2016 titled “A Camelot of the Biomedical Sciences: The Story of the Roche Institute of Molecular Biology”.[14]
After the RIMB closed, in 1997 he accepted a position as distinguished research professor at Florida Atlantic University (FAU) REFF, where he founded, and was director, of the Center for Molecular Biology and Biotechnology [15] (CMBB) for 20 years. In 2017 he was appointed Distinguished Research Professor Emeritus at FAU. His most recent research has involved understanding the mechanisms that cells use to protect against oxidative damage, based on the observation that cells have a mechanism to protect against oxidative damage to methionine residues in proteins [16][17][18][19][20][21][22][23]
Notable awards
Election to the National Academy of Sciences (1982–Present)[24]
300 most cited authors (1961-1976), Current Content July 10, 1978
Superior Service Award of the Department of Health Education and Welfare (1968)
↑ weissbach, H (1967). "Isolation of methyl-B-12 from Escherichia coli B N-5-methyl-H-4-folate-homocysteine vitamin-B-12 transmethylase". Biochemical and Biophysical Research Communications. 27 (3): 398–404. doi:10.1016/s0006-291x(67)80113-x. PMID5340657.
↑ weissbach, H (1966). "Formylation of amino acid analogues of methionine sRNA". Biochemical and Biophysical Research Communications. 24 (1): 50–5. doi:10.1016/0006-291x(66)90408-6. PMID5338733.
↑ Weissbach, H (1970). "Studies on the Purification and Properties of Factor Tu from E. coli". Archives of Biochemistry and Biophysics. 141 (1): 26–37. doi:10.1016/0003-9861(70)90102-5. PMID4921066.
↑ Weissbach, H (1981). "In vitro synthesis of biologically active human leukocyte interferon directed by recombinant plasmid DNA". Archives of Biochemistry and Biophysics. 210 (1): 417–9. doi:10.1016/0003-9861(81)90205-8. PMID6170264.
↑ Weissbach, Herbert; Fisher, David (2016-10-17). A Camelot of the Biomedical Sciences: The Story of the Roche Institute of Molecular Biology. RIMB adventures. ISBN978-0998278407.
↑ Weissbach, H (1992). "High Level Expression and Purification of Peptide Methionine Sulfoxide Reductase in Escherichia coli". Cellular and Molecular Biology. 38 (5): 529–42. PMID1468111.
↑ Weissbach, H (2000). "Structure and mechanism of methionine sulfoxide reductase, an "anti-oxidation" enzyme". Biochemistry. 39 (44): 13307–12. doi:10.1021/bi0020269. PMID11063566.
Dihydrofolate reductase, or DHFR, is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as an electron donor, which can be converted to the kinds of tetrahydrofolate cofactors used in 1-carbon transfer chemistry. In humans, the DHFR enzyme is encoded by the DHFR gene. It is found in the q14.1 region of chromosome 5.
Ceruloplasmin is a ferroxidase enzyme that in humans is encoded by the CP gene.
Methionine synthase also known as MS, MeSe, MTR is responsible for the regeneration of methionine from homocysteine. In humans it is encoded by the MTR gene (5-methyltetrahydrofolate-homocysteine methyltransferase). Methionine synthase forms part of the S-adenosylmethionine (SAMe) biosynthesis and regeneration cycle, and is the enzyme responsible for linking the cycle to one-carbon metabolism via the folate cycle. There are two primary forms of this enzyme, the Vitamin B12 (cobalamin)-dependent (MetH) and independent (MetE) forms, although minimal core methionine synthases that do not fit cleanly into either category have also been described in some anaerobic bacteria. The two dominant forms of the enzymes appear to be evolutionary independent and rely on considerably different chemical mechanisms. Mammals and other higher eukaryotes express only the cobalamin-dependent form. In contrast, the distribution of the two forms in Archaeplastida (plants and algae) is more complex. Plants exclusively possess the cobalamin-independent form, while algae have either one of the two, depending on species. Many different microorganisms express both the cobalamin-dependent and cobalamin-independent forms.
Decorin is a protein that in humans is encoded by the DCN gene.
Beta-hexosaminidase subunit beta is an enzyme that in humans is encoded by the HEXB gene.
Methylmalonyl-CoA mutase (EC 5.4.99.2, MCM), mitochondrial, also known as methylmalonyl-CoA isomerase, is a protein that in humans is encoded by the MUT gene. This vitamin B12-dependent enzyme catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA in humans. Mutations in MUT gene may lead to various types of methylmalonic aciduria.
In enzymology, a 5-methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase is an enzyme that catalyzes the chemical reaction
[Methionine synthase] reductase, or Methionine synthase reductase, encoded by the gene MTRR, is an enzyme that is responsible for the reduction of methionine synthase inside human body. This enzyme is crucial for maintaining the one carbon metabolism, specifically the folate cycle. The enzyme employs one coenzyme, flavoprotein.
In enzymology, a L-methionine (S)-S-oxide reductase (EC 1.8.4.13) is an enzyme that catalyzes the chemical reaction
In enzymology, a peptide-methionine (R)-S-oxide reductase (EC 1.8.4.12) is an enzyme that catalyzes the chemical reaction
Adrenal ferredoxin is a protein that in humans is encoded by the FDX1 gene. In addition to the expressed gene at this chromosomal locus (11q22), there are pseudogenes located on chromosomes 20 and 21.
Peptide methionine sulfoxide reductase (Msr) is a family of enzymes that in humans is encoded by the MSRA gene.
In molecular biology, the (ADP-ribosyl)hydrolase (ARH) family contains enzymes which catalyses the hydrolysis of ADP-ribosyl modifications from proteins, nucleic acids and small molecules.
Methionine sulfoxide is the organic compound with the formula CH3S(O)CH2CH2CH(NH2)CO2H. It is an amino acid that occurs naturally although it is formed post-translationally.
Peptide-methionine (S)-S-oxide reductase (EC 1.8.4.11, MsrA, methionine sulphoxide reductase A, methionine S-oxide reductase (S-form oxidizing), methionine sulfoxide reductase A, peptide methionine sulfoxide reductase, formerly protein-methionine-S-oxide reductase) is an enzyme with systematic name peptide-L-methionine:thioredoxin-disulfide S-oxidoreductase (L-methionine (S)-S-oxide-forming). This enzyme catalyses the following chemical reaction
Rowena Green Matthews, born in 1938, is the G. Robert Greenberg Distinguished University professor emeritus at the University of Michigan, Ann Arbor. Her research focuses on the role of organic cofactors as partners of enzymes catalyzing difficult biochemical reactions, especially folic acid and cobalamin. Among other honors, she was elected to the National Academy of Sciences in 2002 and the Institute of Medicine in 2004.
Charles Clifton Richardson is an American biochemist and professor at Harvard University. Richardson received his undergraduate education at Duke University, where he majored in medicine. He received his M.D. at Duke Medical School in 1960. Richardson works as a professor at Harvard Medical School, and he served as editor/associate editor of the Annual Review of Biochemistry from 1972 to 2003. Richardson received the American Chemical Society Award in Biological Chemistry in 1968, as well as numerous other accolades.
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Bettie Sue Siler Masters is an adjunct professor at Duke University known for her work on nitric oxide synthase and cytochrome P450 reductase. She was the 1992 recipient of the FASEB Excellence in Science Award, and has been elected as a member of the National Academy of Medicine and as a fellow of the American Association for the Advancement of Science.
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