Bettie Sue Masters

Last updated
Bettie Sue Masters
BettieSueMasters in 2013.jpg
Born1937 (age 85–86)
Lexington, Virginia
Alma mater
Scientific career
Fields Biochemistry
Thesis The mechanism of hepatic microsomal triphosphopyridine nucleotide-cytochrome c reductase  (1963)

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. [1]

Contents

Early life and education

Masters was born in Lexington, Virginia, where her father was a radio announcer and a singer. As a child she was an avid reader of Sherlock Holmes and Dr. Watson whose analytical skills she admired. [2] She became interested in chemistry during her sophomore year in high school, and placed high enough in the Westinghouse Science Talent Search to receive a scholarship for college. After the College of William & Mary would not accept the scholarship because she was a woman, she went on to attend Roanoke College, thereby becoming a first-generation college student. [2] She graduated from Roanoke College in 1959 with a B.S. in chemistry. [3] In 1963, she earned her Ph.D. in biochemistry from Duke University. [4]

Career

Following her Ph.D. work, she conducted postdoctoral research first with fellowship support from the American Cancer Society and then with grant support from the American Heart Association. [3] [2] In 1968, she moved to the University of Texas Southwestern Medical School where she started her research lab. [3] [5] In 1982, she moved to the Medical College of Wisconsin to accept the position as chair of the department of biochemistry, thereby becoming the first woman to hold this position. [3] In 1990, she moved to the University of Texas Health Science Center at San Antonio where she was named as the Robert A. Welch Distinguished Professor in Chemistry. [3] As of 2022, she is an adjunct professor at Duke University in the department of biochemistry. [5]

Research

Masters is known for her work on the structure and function of enzymes. As a graduate student she characterized cytochrome P450 reductase (NADPH-cytochrome P450 oxidoreductase). [6] [7] She went on to develop methods to purify enzymes, such as cytochrome P450 reductase, which allows investigation into their biochemical properties [8] and identification of the active sites of the protein through x-ray crystallography. [9] Concerning nitric oxide synthase, she examined the atomic structure of the endothelial isoenzyme, the zinc bound within the protein, and the co-factors required (heme and tetrahydrobiopterin). [10] [11]

Selected publications

Awards and honors

Masters has received numerous honors and awards from Roanoke College, her alma mater. In 1973, she was awarded the Roanoke College Medal for her distinguished service to her community and her profession. [3] In 1983, she received an Honorary Doctor of Science degree from Roanoke College. [3]

In 1990, Masters was recruited to the University of Texas Health Science Center at San Antonio as the first Robert A. Welch Distinguished Professor in Chemistry. [3] In 1992, Masters received the Excellence in Science Award from the Federation of American Societies for Experimental Biology (FASEB). In 2000, she was the recipient of the Bernard B. Brodie Award in Drug Metabolism from the American Society for Pharmacology and Experimental Therapeutics. [12] In 1996, Masters was elected as a member of the National Academy of Medicine [13] and, in 2001, she was elected as a fellow of the American Association for the Advancement of Science. [3] [14] In 2005, Charles University (Prague) awarded Masters an honorary degree, Doctorem Medicinae Honoris Causae, in recognition of her work. [2] In 2022, the Medical College of Wisconsin (MCW) awarded Masters an Honorary Doctor of Science degree in recognition of her leadership role in the field of biochemistry and her contributions to medical scientist training (via initiation of MCW's MD/PhD training program--Medical Scientist Training Program). [15] [16]

Related Research Articles

<span class="mw-page-title-main">Cytochrome</span> Redox-active proteins containing a heme with a Fe atom as a cofactor

Cytochromes are redox-active proteins containing a heme, with a central iron (Fe) atom at its core, as a cofactor. They are involved in electron transport chain and redox catalysis. They are classified according to the type of heme and its mode of binding. Four varieties are recognized by the International Union of Biochemistry and Molecular Biology (IUBMB), cytochromes a, cytochromes b, cytochromes c and cytochrome d.

<span class="mw-page-title-main">Cytochrome P450</span> Class of enzymes

Cytochromes P450 are a superfamily of enzymes containing heme as a cofactor that mostly, but not exclusively, function as monooxygenases. In mammals, these proteins oxidize steroids, fatty acids, and xenobiotics, and are important for the clearance of various compounds, as well as for hormone synthesis and breakdown. In 1963, Estabrook, Cooper, and Rosenthal described the role of CYP as a catalyst in steroid hormone synthesis and drug metabolism. In plants, these proteins are important for the biosynthesis of defensive compounds, fatty acids, and hormones.

<span class="mw-page-title-main">Nitric oxide synthase</span> Enzyme catalysing the formation of the gasotransmitter NO(nitric oxide)

Nitric oxide synthases (NOSs) are a family of enzymes catalyzing the production of nitric oxide (NO) from L-arginine. NO is an important cellular signaling molecule. It helps modulate vascular tone, insulin secretion, airway tone, and peristalsis, and is involved in angiogenesis and neural development. It may function as a retrograde neurotransmitter. Nitric oxide is mediated in mammals by the calcium-calmodulin controlled isoenzymes eNOS and nNOS. The inducible isoform, iNOS, involved in immune response, binds calmodulin at physiologically relevant concentrations, and produces NO as an immune defense mechanism, as NO is a free radical with an unpaired electron. It is the proximate cause of septic shock and may function in autoimmune disease.

<span class="mw-page-title-main">Flavin adenine dinucleotide</span> Redox-active coenzyme

In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may be in the form of FAD or flavin mononucleotide (FMN). Many flavoproteins are known: components of the succinate dehydrogenase complex, α-ketoglutarate dehydrogenase, and a component of the pyruvate dehydrogenase complex.

<span class="mw-page-title-main">Flavoprotein</span> Protein family

Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin. These proteins are involved in a wide array of biological processes, including removal of radicals contributing to oxidative stress, photosynthesis, and DNA repair. The flavoproteins are some of the most-studied families of enzymes.

<span class="mw-page-title-main">Heme oxygenase</span>

Heme oxygenase, or haem oxygenase, is an enzyme that catalyzes the degradation of heme to produce biliverdin, ferrous ion, and carbon monoxide.

Any enzyme system that includes cytochrome P450 protein or domain can be called a P450-containing system.

<span class="mw-page-title-main">Cholesterol side-chain cleavage enzyme</span> Mammalian protein found in Homo sapiens

Cholesterol side-chain cleavage enzyme is commonly referred to as P450scc, where "scc" is an acronym for side-chain cleavage. P450scc is a mitochondrial enzyme that catalyzes conversion of cholesterol to pregnenolone. This is the first reaction in the process of steroidogenesis in all mammalian tissues that specialize in the production of various steroid hormones.

<span class="mw-page-title-main">Cytochrome P450 reductase</span> Mammalian protein found in Homo sapiens

Cytochrome P450 reductase is a membrane-bound enzyme required for electron transfer from NADPH to cytochrome P450 and other heme proteins including heme oxygenase in the endoplasmic reticulum of the eukaryotic cell.

<span class="mw-page-title-main">(Methionine synthase) reductase</span> Class of enzymes

[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.

<span class="mw-page-title-main">NADPH—hemoprotein reductase</span> Enzyme

In enzymology, a NADPH—hemoprotein reductase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Adrenodoxin reductase</span> Protein-coding gene in the species Homo sapiens

Adrenodoxin reductase, was first isolated from bovine adrenal cortex where it functions as the first enzyme in the mitochondrial P450 systems that catalyze essential steps in steroid hormone biosynthesis. Examination of complete genome sequences revealed that adrenodoxin reductase gene is present in most metazoans and prokaryotes.

Flavoprotein pyridine nucleotide cytochrome reductases catalyse the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. The enzymes include ferredoxin-NADP+ reductases, plant and fungal NAD(P)H:nitrate reductases, cytochrome b5 reductases, cytochrome P450 reductases, sulphite reductases, nitric oxide synthases, phthalate dioxygenase reductase, and various other flavoproteins.

Oxidoreductase NAD-binding domain is an evolutionary conserved protein domain present in a variety of proteins that include, bacterial flavohemoprotein, mammalian NADH-cytochrome b5 reductase, eukaryotic NADPH-cytochrome P450 reductase, nitrate reductase from plants, nitric-oxide synthase, bacterial vanillate demethylase and others.

Nitric oxide reductase (NAD(P), nitrous oxide-forming) (EC 1.7.1.14, fungal nitric oxide reductase, cytochrome P450nor, NOR (ambiguous)) is an enzyme with systematic name nitrous oxide:NAD(P) oxidoreductase. This enzyme catalyses the following chemical reaction

(+)-Menthofuran synthase (EC 1.14.13.104, menthofuran synthase, (+)-pulegone 9-hydroxylase, (+)-MFS, cytochrome P450 menthofuran synthase) is an enzyme with systematic name (+)-pulegone,NADPH:oxygen oxidoreductase (9-hydroxylating). This enzyme catalyses the following chemical reaction

Biflaviolin synthase (EC 1.14.21.7, CYP158A2, CYP 158A2, cytochrome P450 158A2) is an enzyme with systematic name flaviolin,NADPH:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Cytochrome P450 aromatic O-demethylase</span>

Cytochrome P450 aromatic O-demethylase is a bacterial enzyme that catalyzes the demethylation of lignin and various lignols. The net reaction follows the following stoichiometry, illustrated with a generic methoxy arene:

Cytochrome P450 BM3 is a Prokaryote Cytochrome P450 enzyme originally from Bacillus megaterium catalyzes the hydroxylation of several long-chain fatty acids at the ω–1 through ω–3 positions. This bacterial enzyme belongs to CYP family CYP102, with the CYP Symbol CYP102A1.This CYP family constitutes a natural fusion between the CYP domain and an NADPH-dependent cytochrome P450 reductase.

Cytochrome P450, family 55, also known as CYP55, is a cytochrome P450 family in fungi supposed to derived from horizontal gene transfer of Actinomycetes CYP105 family member in the ancestor of all Dikarya. The first gene identified in this family is the CYP55A1 from Fusarium oxysporum encoding the NADPH dependent reductase of nitrous oxide.

References

  1. ↑ "Bettie Sue Masters, PhD | Duke Department of Biochemistry". www.biochem.duke.edu. Retrieved 2023-05-30.
  2. 1 2 3 4 Masters, Bettie Sue Siler (2009). "A Professional and Personal Odyssey". Journal of Biological Chemistry. 284 (30): 19765–19780. doi: 10.1074/jbc.x109.007518 . ISSN   0021-9258. PMC   2740401 . PMID   19398561.
  3. 1 2 3 4 5 6 7 8 9 "Dr. Bettie S. Masters '59 | Roanoke College". www.roanoke.edu. Retrieved 2022-06-17.
  4. ↑ Masters, Bettie Sue Siler (1963). The mechanism of hepatic microsomal triphosphopyridine nucleotide-cytochrome c reductase ... (Thesis). OCLC   21574619.
  5. 1 2 "Bettie Sue Masters, PhD | Duke Department of Biochemistry". www.biochem.duke.edu. Retrieved 2022-06-17.
  6. ↑ Masters, B S; Kamin, H; Gibson, Q H; Williams, C H (1965-02-01). "Studies on the Mechanism of Microsomal Triphosphopyridine Nucleotide-Cytochrome C Reductase". The Journal of Biological Chemistry. 240 (2): 921–931. doi: 10.1016/S0021-9258(17)45262-8 . ISSN   1083-351X. PMID   14275154.
  7. ↑ Masters, Bettie Sue Siler; Bilimoria, Minoo H.; Kamin, Henry; Gibson, Quentin H. (1965). "The Mechanism of 1- and 2-Electron Transfers Catalyzed by Reduced Triphosphopyridine Nucleotide-Cytochrome c Reductase". Journal of Biological Chemistry. 240 (10): 4081–4088. doi: 10.1016/s0021-9258(18)97152-8 . ISSN   0021-9258. PMID   4378860.
  8. ↑ Yasukochi, Y; Masters, B S (1976). "Some properties of a detergent-solubilized NADPH-cytochrome c(cytochrome P-450) reductase purified by biospecific affinity chromatography". Journal of Biological Chemistry. 251 (17): 5337–5344. doi: 10.1016/s0021-9258(17)33166-6 . ISSN   0021-9258. PMID   821951.
  9. ↑ Wang, Ming; Roberts, David L.; Paschke, Rosemary; Shea, Thomas M.; Masters, Bettie Sue Siler; Kim, Jung-Ja P. (1997-08-05). "Three-dimensional structure of NADPH–cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes". Proceedings of the National Academy of Sciences. 94 (16): 8411–8416. Bibcode:1997PNAS...94.8411W. doi: 10.1073/pnas.94.16.8411 . ISSN   0027-8424. PMC   22938 . PMID   9237990.
  10. ↑ Raman, C.S; Li, Huiying; Martásek, Pavel; Král, Vladimir; Masters, Bettie Sue S; Poulos, Thomas L (1998). "Crystal Structure of Constitutive Endothelial Nitric Oxide Synthase". Cell. 95 (7): 939–950. doi: 10.1016/s0092-8674(00)81718-3 . ISSN   0092-8674. PMID   9875848. S2CID   2838840.
  11. ↑ Vásquez-Vivar, Jeannette; Kalyanaraman, B.; Martásek, Pavel; Hogg, Neil; Masters, Bettie Sue Siler; Karoui, Hakim; Tordo, Paul; Pritchard, Kirkwood A. (1998-08-04). "Superoxide generation by endothelial nitric oxide synthase: The influence of cofactors". Proceedings of the National Academy of Sciences. 95 (16): 9220–9225. Bibcode:1998PNAS...95.9220V. doi: 10.1073/pnas.95.16.9220 . ISSN   0027-8424. PMC   21319 . PMID   9689061.
  12. ↑ "Brodie Award Recipients | Drug Metabolism & Disposition". ASPET. Retrieved 2022-11-30.
  13. ↑ "Bettie Sue Masters, Ph.D., D.Sc., M.D. (Hon.)". National Academy of Medicine. Retrieved 2022-06-17.[ permanent dead link ]
  14. ↑ "Historic Fellows | American Association for the Advancement of Science". www.aaas.org. Retrieved 2022-06-17.
  15. ↑ "Honorary Degree Recipients | About MCW". Medical College of Wisconsin. Retrieved 2022-11-27.
  16. ↑ "Awards & Honors | Scholars@Duke". Duke University. Retrieved 2022-11-27.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.