Profile Photo of Mike Benedict

Michael Benedik

Vice Provost & Regents Professor of Biology



Joined the Department in 2004

  • B.A. Biology, 1976, University of Chicago
  • Ph.D. Biology, 1982, Stanford University


  • Vice Provost (7/2015-present)
  • Chief International Officer (2018-present)
  • Dean of Faculties and Associate Provost (1/13-6/15)
  • Interim Dean of Faculties and Associate Provost (7/12-1/13)
  • Faculty Ombuds Officer, Texas A&M University (2010-2013)
  • Speaker of the Texas A&M Faculty Senate, 2011-12
  • Graduate Chair, Department of Biology, Texas A&M (2006-2010)
  • Vice-Chair, Faculty of Genetics, Texas A&M (2004-07)
  • Professor, Department of Biology, Texas A&M (2004-present)
  • Professor of Biology and Biochemistry (University of Houston) (2002-04)
  • Vice-Chair, Department of Biology and Biochemistry (University of Houston) (1994-99; 2000-03)
  • Director, Institute for Molecular Biology (University of Houston) (2001-03)
  • Visiting Scientist (sabbatical) NIH-NICHD, 1993-94
  • Associate Director, Institute for Molecular Biology (University of Houston) (1990-2001)
  • Associate Professor of Biochemical and Biophysical Sciences (University of Houston) (1991-2002)
  • Assistant Professor of Biochemical and Biophysical Sciences (University of Houston) (1989-91)
  • Assistant Professor of Biology, Texas A&M University (1985-89)
  • Associate Director, Laboratory for Cloning and Gene Transfer, Department of Medical Biochemistry and Genetics, Texas A&M College of Medicine (1984-85)
  • Staff Scientist, DNAX Research Institute of Molecular & Cellular Biology,(1982-1984) Palo Alto, CA

Dr. Benedik’s laboratory studies basic biological problems using molecular genetic methods and bacteria.  Most recently his group is developing novel microbial approaches for the biotechnology industry. An example of this work is the genetic engineering of proteins useful to remove the highly toxic chemical cyanide released in waste water after industrial and mining use.

Biotechnology/Bioremediation – Cyanide

The aim of this project is better enzymes for degrading cyanide in waste streams and contaminated sites. The industrial uses of cyanide have resulted in contamination at many sites, especially the water and soil of metal plating plants and as the result of ore extraction in mining operations. Especially in light of recent highly-publicized incidents of cyanide contamination (e.g., in Houston-area plating facilities as well as the recent cyanide release in Eastern Europe) there is a need to develop lower-cost, efficient methods to detoxify these sites. Cyanide is a common constituent of biological systems and is actually produced by a variety of organisms, especially plants. Due to the toxicity of cyanide, nature has evolved numerous biochemical pathways for its conversion to innocuous byproducts. There is previous work on biodegradation of cyanide, either by enzymes or metabolically-active whole cells, using a variety of different pathways. The most interesting for our project are those cyanide-degrading enzymes which can function without the need for active cellular metabolism, and can be used under conditions which would kill microorganisms.

We hope to apply modern molecular biology to improve the cost, stability, and metal-tolerance of cyanidases, enzymes which convert cyanide directly to formate and ammonia. These end products are vastly less toxic than cyanide, and they can also be directly metabolized by indigenous microorganisms to cell mass, CO2, and water. Like other enzymes, cyanidases are capable of scavenging and destroying their substrate (i.e., cyanide) down to extremely low levels (< 0.01 ppm). Cyanidases have already been applied to cyanide removal, but the commercial technology is relatively old, and has not taken advantage of: (1) the ability to overexpress enzyme activities in alternative hosts, (2) opportunities for functional improvement by protein engineering, and (3) the discovery and cloning (by others in the literature) of new forms of this enzyme with potentially superior properties.

Our work is leading to further insights on the structural biology of this important branch of nitrilase enzymes as well as in the development of novel enzymes for industrial applications in bioremediation.

Bacterial Persistence and Antibiotic Tolerance

Antibiotics are effective at killing most bacteria, however for any large population there are always a small number of survivors no matter how long the treatment is administered. These bacterial cells that survive antibiotic treatment are called persisters and the phenomenon of bacterial persistence is long-standing. The project aims to elucidate the molecular mechanisms of dormancy in bacteria where bacteria are not killed by antibiotics but rather persist throughout treatment and awaken after the antibiotic therapy ceases. This leads to disease recurrence as well as increased antimicrobial resistance. The project aims to understand the signals that lead to the dormant state and eventually to develop therapeutic interventions that can “wake” these bacteria before antibiotic therapy ceases.

  1. Yamasaki, R, Song, S, Benedik, MJ, Wood, TK. Persister Cells Resuscitate Using Membrane Sensors that Activate Chemotaxis, Lower cAMP Levels, and Revive Ribosomes. iScience. 2020;23 (1):100792. doi: 10.1016/j.isci.2019.100792. PubMed PMID:31926430 PubMed Central PMC6957856.
  2. Benedik, MJ, Sewell, BT. Cyanide-degrading nitrilases in nature. J. Gen. Appl. Microbiol. 2018;64 (2):90-93. doi: 10.2323/jgam.2017.06.002. PubMed PMID:29311498 .
  3. Park, JM, Trevor Sewell, B, Benedik, MJ. Cyanide bioremediation: the potential of engineered nitrilases. Appl. Microbiol. Biotechnol. 2017;101 (8):3029-3042. doi: 10.1007/s00253-017-8204-x. PubMed PMID:28265723 .
  4. Park, JM, Ponder, CM, Sewell, BT, Benedik, MJ. Residue Y70 of the Nitrilase Cyanide Dihydratase from Bacillus pumilus Is Critical for Formation and Activity of the Spiral Oligomer. J. Microbiol. Biotechnol. 2016;26 (12):2179-2183. doi: 10.4014/jmb.1606.06035. PubMed PMID:27586531 .
  5. Crum, MA, Sewell, BT, Benedik, MJ. Bacillus pumilus Cyanide Dihydratase Mutants with Higher Catalytic Activity. Front Microbiol. 2016;7 :1264. doi: 10.3389/fmicb.2016.01264. PubMed PMID:27570524 PubMed Central PMC4981594.
  6. Park, JM, Mulelu, A, Sewell, BT, Benedik, MJ. Probing an Interfacial Surface in the Cyanide Dihydratase from Bacillus pumilus, A Spiral Forming Nitrilase. Front Microbiol. 2015;6 :1479. doi: 10.3389/fmicb.2015.01479. PubMed PMID:26779137 PubMed Central PMC4700190.
  7. Islam, S, Benedik, MJ, Wood, TK. Orphan toxin OrtT (YdcX) of Escherichia coli reduces growth during the stringent response. Toxins (Basel). 2015;7 (2):299-321. doi: 10.3390/toxins7020299. PubMed PMID:25643179 PubMed Central PMC4344625.
  8. Crum, MA, Park, JM, Sewell, BT, Benedik, MJ. C-terminal hybrid mutant of Bacillus pumilus cyanide dihydratase dramatically enhances thermal stability and pH tolerance by reinforcing oligomerization. J. Appl. Microbiol. 2015;118 (4):881-9. doi: 10.1111/jam.12754. PubMed PMID:25597384 .
  9. Crum, MA, Park, JM, Mulelu, AE, Sewell, BT, Benedik, MJ. Probing C-terminal interactions of the Pseudomonas stutzeri cyanide-degrading CynD protein. Appl. Microbiol. Biotechnol. 2015;99 (7):3093-102. doi: 10.1007/s00253-014-6335-x. PubMed PMID:25549622 .
  10. Kwan, BW, Lord, DM, Peti, W, Page, R, Benedik, MJ, Wood, TK et al.. The MqsR/MqsA toxin/antitoxin system protects Escherichia coli during bile acid stress. Environ. Microbiol. 2015;17 (9):3168-81. doi: 10.1111/1462-2920.12749. PubMed PMID:25534751 .
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