Recommended Reading

A running list of recently published papers of interest to the Burstyn Group. Suggestions for this list should be sent to Hannah


1. Koutmos, M., Kabil, O., Smith, J. L., and Banerjee, R. (2010) Structural basis for substrated activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine β-synthase, Proc. Natl. Acad. Sci. U.S.A. 107, 20958-20963.

2. Majtan, T., and Kraus, J. P. (2012) Folding and activity of mutant cystathionine β-synthase depends on the position and nature of the purification tag: Characterization of the R266K CBS mutant, Protein Expression and Purification 82, 317-324.

3. Karunakaran, V., Benabbas, A., Sun, Y., Zhang, Z., Singh, S., Banerjee, R., and Champion, P. M. (2010) Investigations of Low-Frequency Vibrational Dynamics and Ligand Binding Kinetics of Cystathionine β-Synthase, The Journal of Physical Chemistry B 114, 3294-3306.

4. Yammamoto, T., Takano, N., Ishiwata, K., Suematsu, M. (2011) Carbon Monoxide Stimulates Global Protein Methylation via its Inhibitory Action on Cystathionine beta-Synthase. J. Clin. Biochem. Nutr. 96-100.

5. Gupta, S. Kruger, W.D. (2011) Cystathionine beta-Synthase Deficiency Causes Fat Loss in Mice. PLoS One. 6(11)e27598.

6. Hnizda, A., Spiwok, V., Jurga, V., Kozich, V., Kodicek, M., Kraus, J.P. (2010). Cross-talk Between the Catalytic Core and the Regulatory Domain in Cystathionine beta-Synthase: Study by Differential Covalent Labeling and Computational Modeling. Biochemistry. 49(49), 10526-34.

7. Baykov, A. A., Tuominen, H. K., Lahti, R. (2011) The CBS Domain: a Protein Module with an Emerging Prominent Role in Regulation. ACS Chem. Biol. 6(11), 1156-63.

8. Hnízda, A.; et al. (2012), Conformational Properties of Nine Purified Cystathionine β-Synthase Mutants. Biochemistry.

9. Yadav, P.K.; Xie, P.; Banerjee, R. (2012) Allosteric Communication Between the Pyridoxal 5'-Phosphate (PLP) and Heme Sites in the H2S Generator Human Cystathionine β-Synthase. J. Biol. Chem. 287(45), 37611-37620

10. Oyenarte, I.; Majtan, T.; Ereno, J.; Angeles Corral-Rodriguez, M.; Klaudiny, J.; Majtan, J.; Kraus, J.P; Martinez-Cruz, L.A. (2012) Purification, Crystallization, and Preliminary Crystallographic Analysis of the Full-Length Cystathionine β-Synthase from Apis mellifera. Acta Cryst. F68, 1323-1328.

11. Oyenartes, I; Majtan, T.; Erno, J.; Corral-Rodriguez, M.A.; Kraus, J.P.; and Martiniez-Cruz, L.A. (2012) Purification, Crystallization and Preliminary Crystallographic Analysis of Human Cystathionine beta-Synthase. Acta Cyst. F68, 1318-1322.

12. Smith, D.E.C.; Mendes, M.I.S.; Kluitjtmans, L.A.J.; Janssen, M.C.H.; Smulders, Y.M.; Blom, H.J. (2012) A Liquid Chromatography Mass Spectrometry Method for the Measurement of Cystathionine β-Synthase Activity in Cell Extracts. J. Chromatogr. B. 911, 186-191.

13. Carballal, S.; Cuevasanta, E.; Marmisolle, I.; Kabil, O.; Gerasim, C.; Ballous, D.P.; Banerjee, R.; Alvarez, B.; (2013) Kinetics of Reversible Reductive Carbonylation of Heme in Human Cystathionine beta-Synthase. Biochem. 52(26) 4553-4562.

14. Ereno-Orbea, J.; Majtan, T.; Oyenarte, I.; Kraus, J.P.; Martinez-Cruz, L.A.; (2013) Structural Basis of Regulation and Oligomerization of Human Cystathionine beta-Synthase, the Central Enzyme of Transsulfuration. PNAS, ASAP

15. Dimster-Denk, D.; Tripp, K.W.; Marini, N.J.; Marqusee, S.; Rine, J.; (2013) Mono and Dual Cofactor Dependence of Human Cystathionine beta-Synthase Enzyme Variants In Vivo and In Vitro. G3-Genes Genomes Genet. 3(10). 1619-1628.

16. Ereno-ORbea, J.; Oyenarte, I.; Martinez-Cruz, L.A.; (2013) CBS domains: Ligand binding sites and conformational variabilty. Arch. Biochem. Biophys. 540(1-2), 70-81.

17. Gherasim, C.; Yadav, P.K.; Kabil, O.; Niu, W.N.; Banerjee, R.; (2014) Nitirite Reductase Activity and Inhibition of H2S Biogenesis by Human Cystathionine beta-Synthase. PLOS One, 9(1).

18. Mendes, M. I. S.; Colaco, H. G.; Smith, D. E. C.; Ramos, R.; Pop, A.; van Dooren, S. J. M.; de Almeida, I. T.; Kluijtmans, L. A. J.; Janssen, M. C. H.; Rivera, I.; Salomons, G. S.; Leandro, P.; Blom, H. J., (2104) Reduced response of Cystathionine Beta-Synthase (CBS) to S-Adenosylmethionine (SAM): Identification and functional analysis of CBS gene mutations in Homocystinuria patients. J. Inherit. Metab. Dis. 37 (2), 245-254.

19. Vicente, J.B.; Colaco, H.G.; Mendes, M.I.S.; Sarti, P.; Leandro, P.; Giuffre, A.; (2014) NO Binds Human Cystathionine beta-Synthase Quickly and Tightly. J. Biol. Chem. 289(12), 8579-8587.

Gas-Regulated Transcription Factors:

1. Brown, J. H. (2012) Deriving How Far Structural Information is Transmitted Through Parallel Homodimeric Coiled Coils: A correlation analysis of helical staggers. Proteins. doi: 10.1002/prot.24218.

2. Ishida, T.; Aono, S.; (2013) A Model Theoretical Study on Ligand Exchange Reactions of CooA. PCCP, 15(16), 6139-6148.\

3. Levy, C.; Pike, K.; Heyes, D.J.; Joyce, M.G.; Gabor, K.; Smidt, H.; van der Oost, J.; Leys, D.; (2008) Molecular Basis of Haloresipration control by CprK, a CRP-FNR type transcriptional regulator. Mol. Microbio. 70(1) 151-167.

4. Otomo, A.; Ishikawa, H.; Mizuno, M.; Mizutani, Y.; Aono, S.; (2014) Structural Changesin the Heme and Heme Pocket upon CO Dissociation of CooA Observed by Time-Resolved Resonance Raman Spectroscopy. J. Biol. Inorg. Chem. 19, S287.

5. Matta-Camacho, E.; Banerjee, S.; Hughes, T.S.; Solt, L.A.; Wang, Y.; Burris, T.P.; Kojetin, D.J.; (2014) Structure of REV-ERBß Ligand-Binding Domian Bound to a Porphyrin Antagonist. J. Biol. Chem.   ASAP.


Other Hemoproteins:

1. Tsai, A.-L., Berka, V., Martin, E., and Olson, J. S. (2012) A "Sliding Scale Rule" for Selectivity among NO, CO, and O2 by Heme Protein Sensors, Biochemistry 51, 172-186.

2. Winter, M. B., Herzik Jr., M. A., Kuriyan, J., and Marletta, M. A. (2011) Tunnels modulate ligand flux in a heme nitric oxide/oxygen binding (H-NOX) domain, Proc. Natl. Acad. Sci. U.S.A. 108, E881-E889.

3. Muralidharan, S., and Boon, E. M. (2012) Heme Flattening Is Sufficient for Signal Transduction in the H-NOX Family, J. Am. Chem. Soc. 134, 2044-2046.

4. Shimizu, T. (2011) Binding of cysteine thiolate to the Fe(III) heme complex is critical for the function of heme sensor proteins, J. Inorg. Biochem. doi:10.1016/j.jinorgbio.2011.08.018.

5. El-Mashtoly, S. F., Kubo, M., Nakashima, S., Shimizu, T., and Kitagawa, T. (2011) Structural Dynamics of EcDOS Heme Domain Revealed by Time-Resolved Ultraviolet Resonance Raman Spectroscopy, J. Phys. Chem. Lett. 2, 2212-2217.

6. Jones, E. M.; Balakrishnan, G.; Spiro, T. G., Heme Reactivity is Uncoupled from Quaternary Structure in Gel-Encapsulated Hemoglobin: A Resonance Raman Spectroscopic Study. Journal of the American Chemical Society 2012.

7. Murakawa, Y.; Nagai, M.; Mizutani, Y., Differences between Protein Dynamics of Hemoglobin upon Dissociation of Oxygen and Carbon Monoxide. Journal of the American Chemical Society 2012, 134 (3), 1434-1437.

8. Nuernberger, P.; Lee, K. F.; Bonvalet, A.; Bouzhir-Sima, L.; Lambry, J. C.; Liebl, U.; Joffre, M.; Vos, M. H., Strong Ligand-Protein Interactions Revealed by Ultrafast Infrared Spectroscopy of CO in the Heme Pocket of the Oxygen Sensor FixL. Journal of the American Chemical Society 2011, 133 (43), 17110-17113.

10. Vos, M. H.; Bouzhir-Sima, L.; Lambry, J.-C.; Luo, H.; Eaton-Rye, J. J.; Ioanoviciu, A.; Ortiz de Montellano, P. R.; Liebl, U., (2011) Ultrafast Ligand Dynamics in the Heme-Based GAF Sensor Domains of the Histidine Kinases DosS and DosT from Mycobacterium tuberculosis. Biochemistry.

11. Owens, C.P.; Du J.; Dawson, J. H.; Goulding, C. W. (2012) Characterization of Heme Ligation Properities of Rv0203, a Secreted Heme Binding Protein Involved in Mycobacterium tuberculosis Heme Uptake. Biochemistry. 51(7), 1518-31.

12. Yin, L.; Dragnea, V.; and Bauer, C. E. (2012) PpsR, A Regulator of Heme and Bacteriochlorophyll Biosynthesis, Is a Heme-sensing Protein. J. Biol. Chem. 287 (17), 13850-13858.

13. Ghosh, A.; and Steuhr, D.J. (2012) Soluble Guanylyl Cyclase Requires Heat Shock Protein 90 for Heme Insertion During Maturation of the NO-active Enzyme. PNAS. 109 (32) 12998-13003.

14. Hannibal, L.; Collins, D.; Brassard, J.; Chakravarti, R.; et al. (2012) Heme Binding Properties of Glyceraldehyde-3-Phosphate Dehydrogenase. Biochemistry. 51(43), 8514-8529.

15. Cáceres, L.; Necakov, A.S.; Schwartz, C.; et al. (2011) Nitric Oxide Coordinates Metabolism, Growth, and Development via the Nuclear Receptor E75. Genes and Development. 25: 1476-1485.

16. Aono, S. (2013) The Dos Family of Globin-Related Sensors Using PAS Domains to Accomodate Haem Aciting as the Active Site for Sensing External Signals. Microbial Globins- Status and Oppertunities. Vol. 63, Academic Press Ltd.-Elsevier Science Ltd., London, 273-327.

17. Rios-Gonzalez, B.B.; Roman-Morales, E.M.; Pietri, R.; Lopez-Garriga, J.; (2014) Hydrogen Sulfide Activation in Hemeproteins: The Sulfheme Scenario. J. Inorg. Biochem. ASAP.

General Interest:

1. Banerjee, R. (2012) Redox outside the Box: Linking Extracellular Redox Remodeling with Intracellular Redox Metabolism, J. Biol. Chem. 287, 4397-4402.

2. Nicoletti, F. P.; Droghetti, E.; Boechi, L.; Bonamore, A.; Sciamanna, N.; Estrin, D. A.; Feis, A.; Boffi, A.; Smulevich, G., (2011) Fluoride as a Probe for H-Bonding Interactions in the Active Site of Heme Proteins: The Case of Thermobifida fusca Hemoglobin. Journal of the American Chemical Society.

3. Rebouças, J. S.; Patrick, B. O.; James, B. R., (2012)Thiol, Disulfide, and Trisulfide Complexes of Ru Porphyrins: Potential Models for Iron–Sulfur Bonds in Heme Proteins. Journal of the American Chemical Society, 134 (7), 3555-3570.

4. Thielges, M. C.; Chung, J. K.; Axup, J. Y.; Fayer, M. D., (2011) Influence of Histidine Tag Attachment on Picosecond Protein Dynamics. Biochemistry.

5. Kerby, R. L., and Roberts, G. P. (2011) Sustaining N2-Dependent Growth in the Presence of CO, J. Bacteriol. 193, 774-777.

6. Morikawa, T. et al. (2012) Hypoxic Regulation of the Cerebral Microcirculation is Mediated by a Carbon Monoxide-Sensitive Hydrogen Sulfide Pathway. Proc. Natl. Acad. Sci. USA. 109 (4), 1293-8.

7. Selwood, T.; Jaffe, E. K., (2012) Dynamic dissociating homo-oligomers and the control of protein function. Archives of Biochemistry and Biophysics , 519 (2), 131-143.

8. Toth-Petroczy, A. and Tawfik, D. (2011) Slow Protein Evolutionary Rates are Dictated By Surface-Core Association. PNAS, 108(27) 11151-11156.

9. Bar-Even, A.; Noor, E.; Savir, Y.; Liebermeister, W.; Davidi, D.; Tawfik, D.; Milo, R. (2011) The Moderately Efficient Enzyme: Evolutionary and Physicochemical Trends Shaping Enzyme Parameters.  Biochemistry, 50, 4402-4410.

10. Jackson, M.R., et al. (2012) Human Sulfide: Quinone Oxidoreductase Catalyzes the First Step in Hydrogen Sulfide Metabolism and Produces a Sulfane Sulfur Metabolite. Biochemistry. ASAP

11. Spiro, T.G.; Soldatova, A.V.; (2012) Ambidentate H-bonding of NO and O-2 in Heme Proteins. J. Inorg. Biol. 115, 204-210.

12. Crawford, R.; Erben, C.M.; Periz, J.; Hall, L.M.; Brown, T.; Tuberfield, A.J.; Kapanidis, A.N. (2013) Non-Covalent Single Transcription Factor Encapsulation Inside a DNA Cage. Angew. Chem. Int. Ed. 52, 1-6 (ASAP).

13. Balakrishnan, G.; Soldatova, A.V.; Spiro, T.G. (2013) CO, NO, and O2 as Vibrational Probes of Heme Protein Interactions. Coord. Chem. Rev. 257(2, SI) 511-527.

14. Chang, C.J.; He, C.; (2013) Using Chemistry to Study and Control Metals in Biology. Curr. Opin. Chem. Biol. ASAP.

15. Girvan, H.M.; Munro, A.W.; (2013) Heme Sensor Proteins. J. Biol.Chem. ASAP.

16. Bonnet, M.; Kurz, M.; Mesa, S.; Briand, C.; Hennecke, H.; Grütter, M.G.; (2013) Structure of Bradyhizobium japonicum Transcription Factor FixK2 Unveils Sites of DNA Binding and Oxidation. J. Biol. Chem. ASAP.

17. Zhao, Y.; Bhushan, S.; Yang, C.; Otsuka, H.; Stein, J.D.; Pacheco, A.; Peng, B.; Devaire-Baez, N.O.; Aguilar, H.C.; Lefer, D.J.; Xian, M.; (2013) Controllable Hydrogen Sulfide Donors and Their Activity Against Myocardial Ischemia-Reperfusion Injury. ACS Chem. Biol. ASAP.

18. Franke, A.; van Eldik, R.; (2013) Factors that Determine the Mechanism of NO Activation by Metal Complexes of Biological and Environmental Relevance. Euro. J. Inorg. Chem. 4, 460-480.

19. Itoh, R.; Fujita, K.; Mu, A.; Kim, D.H.T.; Tai, T.T.; Sagami, I.; Taketani, S.; (2013) Imagining of Heme/Hemeproteins in Nucleus of the Living Cells Expressing Heme-Binding Nuclear Receptors. FEBS Letters. 587(14) 2131-2136.

20. Liebl, U., Lambry, J. C., and Vos, M. H. (2013) Biochimica Et Biophysica Acta-Proteins and Proteomics 1834, 1684-1692

21. Bailey, T.S.; Pluth, M.D.; (2013)Chemiluminescent Detection of Enzymatically Produced Hydrogen Sulfide: Substrate Hydrogen Bonding Influences Selectivity for H2S over Biological Thiols. J. Am. Chem. Soc. ASAP.

22. Weinert, E.E.; Phillips-Piro, C.M.; Marletta, M.A.; (2013) Porphyrin π-stacking in a Heme Protein Scaffold Tunes Gas Ligand Affinity. J. Inorg. Biochem. 127(0), 7-12.

23. Germani, F.; Moens, L.; Dewilde, S.; (2013) Haem-Based Sensors: A Still Growing Old Superfamily. Advances in Microbial Physiology: Microbial Globins- Status and Oppertunities. Vol. 63, Academic Press Ltd.-Elsevier Science Ltd., London, 1-47