Irwin Fridovich

Irwin Fridovich (August 2, 1929 – November 2,

2019)[1] was an American biochemist who, together Irwin Fridovich
with his graduate student Joe M. McCord, discovered
the enzymatic activity of copper-zinc superoxide
dismutase (SOD),[2][3]—to protect organisms from the
toxic effects of superoxide free radicals formed as a
byproduct of normal oxygen metabolism.[4]
Subsequently, Fridovich's research group also
discovered the manganese-containing[5] and the iron-
containing[6] SODs from Escherichia coli and the
mitochondrial MnSOD (SOD2),[7] now known to be Born August 2, 1929
an essential protein in mammals.[8] He spent the rest of New York City, New York, U.S.
his career studying the biochemical mechanisms of
Died November 2, 2019 (aged 90)
SOD and of biological superoxide toxicity, using
Education City College of New York (BS
bacteria as model systems.[9][10][11] Fridovich was also
1951), Duke University (PhD
Professor Emeritus of Biochemistry at Duke
1955)
University.
Known for Superoxide dismutase, oxygen
free radicals
Academic career Awards Elliott Cresson Medal (1997)
Scientific career
From 1951 to 1952, Fridovich served as a medical
Fields Biochemistry
research associate at Cornell Medical College. He held
junior teaching positions in biochemistry at Duke Institutions Cornell Medical College, Duke
University 1956 to 1961 and was a visiting research University
associate at Harvard University from 1961 to 1962. He Doctoral Philip Handler
became an assistant professor in biochemistry at Duke advisor
University in 1961 and a full professor in 1971. He Doctoral Joe M. McCord, Hara P. Misra
was appointed as James B. Duke Professor of students
Biochemistry in 1976 and held the position as
professor emeritus since 1996 until his death.

Awards and honors

Fridovich received numerous awards and recognitions for his work, including membership in the
National Academy of Sciences and the American Academy of Arts and Sciences, and the Elliott Cresson
Medal of the Franklin Institute, Philadelphia. According to Google Scholar, he has over 51,000 citations
in the scientific literature, including 7 papers with >1000 citations, and an h-index of 97.[12] His
discovery of the superoxide dismutase reaction essentially started the field of oxygen free radicals in
biology and medicine,[11][13] and that influence is shown by his election as president of the American
Society of Biological Chemists (for 1982–83)[1] ([Link]
[Link]/uploadedfiles/aboutus/asbmb_history/past_presidents/1980
s/[Link]) Archived ([Link]
20604173903/[Link]
MB_History/Past_Presidents/1980s/[Link]) 2012-06-
04 at the Wayback Machine, the Oxygen Society (1987–1990),
and the Society for Free Radical Research (1992–94), as well as
award of the Science & Humanity Prize at the 2000 Oxygen Club
World Congress.

References Ribbon drawing of the subunit 3D

structure of Cu,Zn superoxide
1. "Duke Flags Lowered: Biochemist Irwin Fridovich Dies at
dismutase
Age 90" ([Link]
red-biochemist-irwin-fridovich-dies-age-90).
2. McCord JM, Fridovich I (1969). "Superoxide Dismutase,
An Enzymic Function for Erythrocuprein (Hemocuprein)"
([Link]
4-5). Journal of Biological Chemistry. 244 (22): 6049–
6055. doi:10.1016/S0021-9258(18)63504-5 ([Link]
rg/10.1016%2FS0021-9258%2818%2963504-5).
PMID 5389100 ([Link]
0).
3. Fridovich I (1998). "The trail to superoxide dismutase" (h
ttps://[Link]/pmc/articles/PMC2143889).
Protein Science. 7 (12): 2688–2690.
doi:10.1002/pro.5560071225 ([Link]
Fpro.5560071225). PMC 2143889 ([Link]
[Link]/pmc/articles/PMC2143889). PMID 9865966 (http
s://[Link]/9865966).
4. Bannister WH, Bannister JV (1988). "Isolation and
characterization of superoxide dismutase: a personal
history and tribute to Joe McCord and Irwin Fridovich".
Free Radical Biology and Medicine. 5 (5–6): 371–6.
doi:10.1016/0891-5849(88)90110-4 ([Link]
16%2F0891-5849%2888%2990110-4). PMID 2855737
([Link]
5. BB Keele Jr; JM McCord; I Fridovich (1970).
"Superoxide Dismutase from Escherichia coli B: A new
manganese-containing enzyme" ([Link]
6%2FS0021-9258%2818%2962675-4). Journal of
Biological Chemistry. 245 (22): 6176–6181.
doi:10.1016/S0021-9258(18)62675-4 ([Link]
1016%2FS0021-9258%2818%2962675-4).
PMID 4921969 ([Link]
9).
 6. FJ Yost Jr; I Fridovich (1973). "An iron-containing superoxide dismutase from Escherichia
coli" ([Link] Journal of Biological
Chemistry. 248 (14): 4905–4908. doi:10.1016/S0021-9258(19)43649-1 ([Link]
16%2FS0021-9258%2819%2943649-1). PMID 4352182 ([Link]
352182).
7. Weisiger RA, Fridovich I (1973). "Superoxide Dismutase: Organelle specificity" ([Link]
g/10.1016%2FS0021-9258%2819%2943969-0). Journal of Biological Chemistry. 248 (10):
3582–3592. doi:10.1016/S0021-9258(19)43969-0 ([Link]
8%2819%2943969-0). PMID 4702877 ([Link]
8. McCord JM, Fridovich I (1988). "Superoxide dismutase: the first twenty years (1968-1988)".
Free Radical Biology and Medicine. 5 (5–6): 363–9. doi:10.1016/0891-5849(88)90109-8 (htt
ps://[Link]/10.1016%2F0891-5849%2888%2990109-8). PMID 2855736 ([Link]
[Link]/2855736).
9. Fridovich I (1978). "The biology of oxygen radicals". Science. 201 (4359): 875–880.
Bibcode:1978Sci...201..875F ([Link]
doi:10.1126/science.210504 ([Link] PMID 210504 (ht
tps://[Link]/210504).
10. Fridovich I (1995). "Superoxide radical and superoxide dismutases" ([Link]
web/20190306211313/[Link]
[Link]) (PDF). Annual Review of Biochemistry. 64: 97–112.
doi:10.1146/[Link].64.070195.000525 ([Link]
5.000525). PMID 7574505 ([Link] S2CID 26834871 (ht
tps://[Link]/CorpusID:26834871). Archived from the original ([Link]
[Link]/d57d/[Link]) (PDF) on 2019-
03-06.
11. Kresge N, Simoni RD, Hill RL (2006). "Forty Years of Superoxide Dismutase Research: the
Work of Irwin Fridovich (JBC Classics: Enzymology)" ([Link]
[Link]). The Journal of Biological Chemistry. 281 (22): e17. doi:10.1016/S0021-
9258(20)56010-9 ([Link] Retrieved
July 3, 2011.
12. "Irwin Fridovich" ([Link]
Google Scholar. Retrieved 3 July 2012.
13. Imlay JA (2011). "Redox pioneer: professor Irwin Fridovich" ([Link]
mc/articles/PMC3026652). Antioxidants & Redox Signaling. 14 (3): 335–40.
doi:10.1089/ars.2010.3264 ([Link] PMC 3026652 (http
s://[Link]/pmc/articles/PMC3026652). PMID 20518701 ([Link]
[Link]/20518701).

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