Myron L. Bender

{{Infobox scientist

|name =Myron Lee Bender

|birth_name =

|birth_date = 1924

|birth_place = St. Louis, Missouri

|death_date = {{death date and age|1988|1924}}

|death_place =

|spouse = Muriel S. Bender

|partner =

|children =

|education = Purdue University (B.S., Ph.D.)

|known_for = Hass–Bender oxidation, studies of enzyme mechanisms

|awards = Midwest Award of the American Chemical Society, 1972.

|child =

|fields = Reaction mechanisms, biochemistry of enzyme action.

|workplaces = Harvard University, University of Connecticut, University of Chicago, Illinois Institute of Technology, Northwestern University

|thesis_title =

|thesis_url =

|thesis_year =

|doctoral_advisor = Henry B. Hass

| academic_advisors = Paul D. Barlett, Frank H. Westheimer

|doctoral_students =

}}

Myron Lee Bender (1924–1988) was born in St. Louis, Missouri. He obtained his B.S. (1944) and his Ph.D. (1948) from Purdue University. The latter was under the direction of Henry B. Hass. After postdoctoral research under Paul D. Barlett (Harvard University), and Frank H. Westheimer (University of Chicago), he spent one year as a faculty member at the University of Connecticut. Thereafter, he was a professor of Chemistry at Illinois Institute of Technology in 1951, and then at Northwestern University in 1960. He worked primarily in the study of reaction mechanisms and the biochemistry of enzyme action. Myron L. Bender demonstrated the two-step mechanism of catalysis for serine proteases, nucleophilic catalysis in ester hydrolysis and intramolecular catalysis in water. He also showed that cyclodextrin can be used to investigate catalysis of organic reactions within the scope of host–guest chemistry. Finally, he and others reported on the synthesis of an organic compound as a model of an acylchymotrypsin intermediate.

During his career, Myron L. Bender was an active member of the Chicago Section of the American Chemical Society. He was elected a Fellow of Merton College, Oxford University, and to the National Academy of Sciences, the latter in 1968. He received an honorary degree from Purdue University in 1969. He was the recipient of the Midwest Award of the American Chemical Society in 1972.

Professor Bender retired from Northwestern in 1988. Both he and his wife, Muriel S. Bender, died that year.

Research

=Research papers=

Bender's initial work concerned mechanisms of chemical reactions,{{cite journal | doi= 10.1021/ja01148a063| title= Oxygen Exchange as Evidence for the Existence of an Intermediate in Ester Hydrolysis| year= 1951| last1= Bender| first1= Myron L.| journal= Journal of the American Chemical Society| volume= 73| issue= 4| pages= 1626–1629| bibcode= 1951JAChS..73.1626B}} and although this continued through his career he became increasingly interested in enzyme mechanisms,{{cite journal | doi= 10.1021/ja01564a035| title= General Basic Catalysis of Ester Hydrolysis and Its Relationship to Enzymatic Hydrolysis1| year= 1957| last1= Bender| first1= Myron L.| last2= Turnquest| first2= Byron W.| journal= Journal of the American Chemical Society| volume= 79| issue= 7| pages= 1656–1662| bibcode= 1957JAChS..79.1656B}} especially that of α-chymotrypsin.{{cite journal | doi= 10.1021/ja01558a030| title= The Kinetics of the α-Chymotrypsin-catalyzed Oxygen Exchange of Carboxylic Acids1| year= 1957| last1= Bender| first1= Myron L.| last2= Kemp| first2= Kenneth C.| journal= Journal of the American Chemical Society| volume= 79| issue= 1| pages= 116–120| bibcode= 1957JAChS..79..116B}}{{cite journal | doi= 10.1021/ja01498a027| title= The Kinetics of the α-Chymotrypsin-catalyzed Hydrolysis and Methanolysis of Acetyl-L-phenylalanine Methyl Ester. Evidence for the Specific Binding of Water on the Enzyme Surface1| year= 1960| last1= Bender| first1= Myron L.| last2= Glasson| first2= William A.| journal= Journal of the American Chemical Society| volume= 82| issue= 13| pages= 3336–3342| bibcode= 1960JAChS..82.3336B}}{{cite journal | doi= 10.1021/ja01471a040| title= The formation of the acyl-enzyme intermediate, trans-cinnamoyl-α-chymotrypsin, in the hydrolyses of non-labile trans-cinnamic acid esters1| year= 1961| last1= Bender| first1= Myron L.| last2= Zerner| first2= Burt| journal= Journal of the American Chemical Society| volume= 83| issue= 10| pages= 2391–2392| bibcode= 1961JAChS..83.2391B}} Later he broadened his interest to encompass other enzymes, such as acetylcholinesterase{{cite journal | doi= 10.1021/ja01085a045| title= Titration of the Active Sites of Acetylcholinesterase| year= 1965| last1= Bender| first1= Myron L.| last2= Stoops| first2= James K.| journal= Journal of the American Chemical Society| volume= 87| issue= 7| pages= 1622–1623| pmid= 14302679| bibcode= 1965JAChS..87.1622B}} and carboxypeptidase,{{cite journal | doi= 10.1073/pnas.53.4.711| title= The Effect of Enzyme Acetylation on the Kinetics of the Carboxypeptidase-A-Catalyzed Hydrolysis of Hippuryl-L-Phenyllactic Acid| year= 1965| last1= Bender| first1= M. L.| last2= Whitaker| first2= J. R.| last3= Menger| first3= F.| journal= Proceedings of the National Academy of Sciences| volume= 53| issue= 4| pages= 711–716| pmid= 14324526| pmc= 221055| doi-access= free}} and others.{{cite journal | doi= 10.1021/ja00976a034| title= The Determination of the Concentration of Hydrolytic Enzyme Solutions: α-Chymotrypsin, Trypsin, Papain, Elastase, Subtilisin, and Acetylcholinesterase| year= 1966| last1= Bender| first1= Myron L.| last2= Begué-Cantón| first2= Maria Luisa Begué| last3= Blakeley| first3= Robert L.| last4= Brubacher| first4= Lewis J.| last5= Feder| first5= Joseph| last6= Gunter| first6= Claude R.| last7= Kézdy| first7= Ferenc J.| last8= Killheffer| first8= John V.| last9= Marshall| first9= Thomas H.| last10= Miller| first10= Charles G.| last11= Roeske| first11= Roger W.| last12= Stoops| first12= James K.| journal= Journal of the American Chemical Society| volume= 88| issue= 24| pages= 5890–5913| pmid= 5980876| bibcode= 1966JAChS..88.5890B}}

Bender pioneered the use of p-nitrophenyl acetate as a model substrate for studying proteolysis, as it is particularly convenient in spectroscopic experiments.{{cite journal | doi= 10.1021/ja01564a034| title= The Imidazole-catalyzed Hydrolysis of p-Nitrophenyl Acetate1| year= 1957| last1= Bender| first1= Myron L.| last2= Turnquest| first2= Byron W.| journal= Journal of the American Chemical Society| volume= 79| issue= 7| pages= 1652–1655| bibcode= 1957JAChS..79.1652B}}{{cite journal | doi= 10.1021/bi00912a021| title= The Kinetics of the α-Chymotrypsin-Catalyzed Hydrolysis of p-Nitrophenyl Acetate| year= 1962| last1= Kezdy| first1= Ferenc J.| last2= Bender| first2= Myron L.| journal= Biochemistry| volume= 1| issue= 6| pages= 1097–1106| pmid= 14032227}} He likewise used imidazole as a model catalyst for shedding light on enzyme action.{{cite journal | doi= 10.1021/ja00883a055| title= Imidazole Catalysis of the Hydrolysis of δ-Thiovalerolactone| year= 1962| last1= Westheimer| first1= F. H.| last2= Bender| first2= Myron L.| journal= Journal of the American Chemical Society| volume= 84| issue= 24| pages= 4908–4909| bibcode= 1962JAChS..84.4908W}}

He also studied artificial enzymes, starting with modified subtilisin in which a serine residue was replaced by cysteine (replacing an ester group with a thiol).{{cite journal | doi= 10.1021/ja00965a060| title= A New Enzyme Containing a Synthetically Formed Active Site. Thiol-Subtilisin1| year= 1966| last1= Polgar| first1= Laszlo| last2= Bender| first2= Myron L.| journal= Journal of the American Chemical Society| volume= 88| issue= 13| pages= 3153–3154| bibcode= 1966JAChS..88.3153P}} Polgar and Bender laid stress on the fact that the modified enzyme was catalytically active,

whereas Koshland and Neet,{{cite journal | doi= 10.1073/pnas.56.5.1606| title= The conversion of serine at the active site of subtilisin to cysteine: A "chemical mutation"| year= 1966| last1= Neet| first1= K. E.| last2= Koshland| first2= D. E.| journal= Proceedings of the National Academy of Sciences| volume= 56| issue= 5| pages= 1606–1611| pmid= 5230319| pmc= 220044| bibcode= 1966PNAS...56.1606N| doi-access= free}} who made essentially the same observation the same year, drew the opposite conclusion, that despite replacing group with one in principle more reactive, the modified enzyme was less effective as a catalyst than the unmodified enzyme. Philipp and Bender later did a detailed study of the catalytic differences between native subtilisin and thiolsubtilisin.{{cite journal | doi=10.1007/BF00215583| title= Kinetics of subtilisin and thiolsubtilisin| year= 1983| last1= Philipp| first1= Manfred| last2= Bender| first2= M. L.| journal= Molecular and Cellular Biochemistry| volume= 51| issue= 1| pages= 5–32| pmid= 6343835| s2cid= 24136200}} Bender also studied other artificial enzymes,{{cite journal | doi= 10.1021/ja00707a046| title= Cycloamyloses as enzyme models. Effects of inclusion complex formation on intramolecular participation| year= 1970| last1= Vander Jagt| first1= David L.| last2= Killian| first2= Frederick L.| last3= Bender| first3= M. L.| journal= Journal of the American Chemical Society| volume= 92| issue= 4| pages= 1016–1022| pmid= 5451006| bibcode= 1970JAChS..92.1016V}} such as cycloamyloses, that were not simply modified natural enzymes.

Bender may have been the first to recognize that the specificity constant ( $k_\mathrm{cat}/K_\mathrm{m}$ , the ratio of catalytic constant to Michaelis constant) provides the best measure of enzyme specificity,{{cite journal | doi= 10.1021/ja01053a050| title= Use of the specificity constant of α-chymotrypsin| year= 1969| last1= Brot| first1= Frederick E.| last2= Bender| first2= Myron L.| journal= Journal of the American Chemical Society| volume= 91| issue= 25| pages= 7187–7191| bibcode= 1969JAChS..91.7187B}} and to use the term specificity constant for it, as later recommended by the IUBMB.{{cite journal | doi= 10.1016/j.pisc.2014.02.006 | title = Current IUBMB recommendations on enzyme nomenclature and kinetics | last1 = Cornish-Bowden | first1 = A. | date = 2014 | journal = Perspectives in Science | volume = 1 | issue = 1–6 | pages=74–87| bibcode = 2014PerSc...1...74C | doi-access = free}} Philipp and Bender proposed that this specificity constant is the same as the second-order rate constant for enzyme-substrate binding{{cite journal | doi= 10.1038/newbio241044a0| title= Is binding the rate-limiting step in acylation of alpha-chymotrypsin by specific substrates?| year= 1973| last1= Philipp| first1= Manfred| last2= Bender| first2= Myron L.| journal= Nature New Biology| volume= 241| issue= 106| page= 44| pmid= 4512333| doi-access= free}} for the most active substrates.

=Reviews=

Bender authored or co-authored several reviews, for example summarizing several years' work on α-chymotrypsin,{{cite journal | doi= 10.1021/ja01072a020| title= The Current Status of the α-Chymotrypsin Mechanism| year= 1964| last1= Bender| first1= Myron L.| last2= Kezdy| first2= Ferenc J.| journal= Journal of the American Chemical Society| volume= 86| issue= 18| pages= 3704–3714| bibcode= 1964JAChS..86.3704B}} and proteolytic enzymes in general.{{cite journal | doi= 10.1146/annurev.bi.34.070165.000405| title= Mechanism of Action of Proteolytic Enzymes| year= 1965| last1= Bender| first1= M. L.| last2= Kezdy| first2= F. J.| journal= Annual Review of Biochemistry| volume= 34| pages= 49–76| pmid= 14321178}}

=Books=

Bender's books primarily concerned catalysis,{{cite book| isbn= 978-0471065005| title= Mechanisms of Homogeneous Catalysis from Protons to Proteins| last1= Bender| first1= Myron L.| year= 1971| publisher= Wiley-Interscience}} especially catalysis by enzymes

{{cite book| isbn= 978-0070044500| title= Catalysis and Enzyme Action| last1= Bender| first1= M. L.| last2= Brubacher| first2= Lewis J.| year= 1973| publisher= McGraw-Hill}} and its underlying chemistry,{{cite book| isbn= 978-0471059912| title= The Bioorganic Chemistry of Enzymatic Catalysis| last1= Bender| first1= Myron L.| last2= Bender| first2= Mike| last3= Bergeron| first3= Raymond J.| last4= Komiyama| first4= Makoto| date= 1984| publisher= Wiley}} and also cyclodextrin chemistry;{{cite book | isbn= 978-3540085775 | title = Cyclodextrin Chemistry | last1= Bender | first1 = Myron L | last2 = Kobiyama | first2 = M. | publisher = Springer-Verlag | place= Berlin | date = 1978}}

Bender Distinguished Summer Lecturers

The series of Myron L. Bender & Muriel S. Bender Distinguished Summer Lectures in Organic Chemistry was established in 1989 and hosted by the Department of Chemistry at Northwestern University. The scientists who have given these lectures include

Julius Rebek (1990),

JoAnne Stubbe (1992),

Peter B. Dervan (1993),

Marye Anne Fox (1994),

Richard Lerner (1995),

Eric Jacobsen (1997),

Larry E. Overman (1998),

Ronald Breslow (1999),

Jean Fréchet (2000),

Dale Boger (2001),

|Barbara Imperiali (2003),

François Diederich (2004),

Christopher T. Walsh (2008),

Stephen L. Buchwald (2009),

Paul Wender (2010), and

Kendall Houk (2011).

References

Northwestern University Department of Chemistry Brochure for the Myron L. Bender & Muriel S. Bender Distinguished Summer Lectures in Organic Chemistry, 2009.
Frank H. Westheimer, Myron L. Bender, in Biographical Memoirs, the National Academy of Sciences (includes photograph of Prof. Bender, last accessed November 28, 2009, http://www.nap.edu/readingroom.php?book=biomems&page=mbender.html)