Ratliff, A.C., Buchanan, S.K., and Celia, H. (2022). The Ton motor. Frontiers Microbiol., in press.
Diederichs, K.A., Pitt, A.S., Varughese, J.T., Hackel, T.N. Buchanan, S.K. & Shaw, P.L. (2022). Mechanistic insights into fungal mitochondrial outer membrane protein biogenesis. Curr Opin Struct Biol, in press.
Varughese, J. Buchanan, S.K. & Pitt, A.S. (2021). The role of Voltage-Dependent Anion Channel in mitochondrial dysfunction and human disease. Cells. 2021 Jul 9;10(7):1737. doi: 10.3390/cells10071737.[LINK]
Pitt, A.S. & Buchanan, S.K. (2021). A biochemical and structural understanding of TOM complex interactions and implications for human health and disease. Cells. 2021 May 11;10(5):1164. doi: 10.3390/cells10051164.[LINK]
Guerin, J. & Buchanan, S.K. (2021). Protein import and export across the bacterial outer membrane. Curr Opin Struct Biol, 69:55-62.doi: 10.1016/j.sbi.2021.03.007.[LINK]
Diederichs, K.A., Buchanan, S.K. & Botos, I. (2121). Building better barrels - β-barrel biogenesis and insertion in bacteria and mitochondria. J Mol Biol 433(16):166894.[LINK]
Kotov, V., Mlynek, G., Vesper, O., Pletzer, M., Wald, J., Teixeira-Duarte, C.M., Celia, H., Garcia-Alai, M., Nussberger, S., Buchanan, S.K., Morais-Cabral, J.H., Loew, C., Djinovic-Carugo, K. & Marlovits, T. (2121). In-depth interrogation of protein thermal unfolding data with MoltenProt. Protein Sci 30:201-217.[LINK]
Guerin, J., Botos, I., Zhang, Z., Lundquist, K., Gumbart, J.C. & Buchanan, S.K. (2020). Structural insight into toxin secretion by contact-dependent growth inhibition transporters. eLife 9:e58100. doi: 10.7554/eLife.58100.[LINK]
Ratliff, A.C., Buchanan, S.K. & Celia, H. (2020). Ton motor complexes. Curr Opin Struct Biol, 67:95-100.[LINK]
Diederichs, K.A., Ni, X., Rollauer, S.E., Botos, I., Tan, X., King, M.S., Kunji, E.R.S., Jiang, J. & Buchanan, S.K. (2020). Structural insight into mitochondrial β-barrel outer membrane protein biogenesis. Nat Commun 11(1): 3290. doi: 10.1038/s41467-020-17144-1.[LINK]
Shaw, P.L.R., Diederichs, K.A., Pitt, A., Rollauer, S.E. & Buchanan, S.K. (2020). Cloning and multi-subunit expression of mitochondrial membrane protein complexes in Saccharomyces cerevisiae. Methods Mol Biol 2127:1-11.[LINK]
Celia, H., Noinaj, N. & Buchanan, S.K. (2020). Structure and stoichiometry of the Ton molecular motor. Int J Mol Sci, Jan 7;21(2). pii: E375. doi: 10.3390/ijms21020375.[LINK]
Celia, H., Botos, I., Ni, X., Fox, T., De Val, N., Lloubles, R., Jiang, J., & Buchanan, S.K. (2019). Cryo-EM structure of the bacterial Ton motor subcomplex ExbB-ExbD provides information on structure and stoichiometry. Commun Biol Oct 4;2:358. doi: 10.1038/s42003-019-0604-2. eCollection 2019.[LINK]
Hoogerheide, D.P., Noskov, S.Y., Kuszak, A.J., Buchanan, S.K., Rostovtseva, T.K. & Nanda, H. (2018). Structure of voltage-dependent anion channel-tethered bilayer lipid membranes determined using neutron reflectivity. Acta Crystallogr D, 74: 1219-1232.[LINK]
Ghequire, M.K.G., Swings, T., Michiels, J., Buchanan, S.K. & De Mot, R. (2018). Hitting with a BAM: Selective killing by lectin-like bacteriocins. MBio 9, pii: e02138-17. doi: 10.1128/mBio.02138-17.[LINK]
Ghequire, M.G.K, Buchanan, S.K. & De Mot, R. (2018). The ColM family, polymorphic toxins breaching the bacterial cell wall. MBio 9, pii: e02267-17. doi: 10.1128/mBio.02267-17.[LINK]
Sikora, A.E., Wierzbicki, I.H., Zielke, R.A., Ryner, R.F., Korotkov, K.V., Buchanan, S.K. & Noinaj, N. (2018). Structural and functional insights into the role of BamD and BamE within the beta-barrel assembly machinery in Neisseria gonorrhoeae. J. Biol. Chem. 293: 1106-1119.[LINK]
Guérin, J., Bigot, S., Schneider, R., Buchanan, S.K. & Jacob-Dubuisson, F. (2017). Two-partner secretion: combining efficiency and simplicity in the secretion of large proteins for bacteria-host and bacteria-bacteria interactions. Front. Cell. Infect. Microbiol. 7:148, doi: 10.3389/fcimb.2017.000148.[LINK]
Botos, I, Noinaj, N. & Buchanan, S.K. (2017). Insertion of proteins and lipopolysaccharide into the bacterial outer membrane. Phil. Trans. R. Soc. B 372: 20160224.[LINK]
Ghequire, M.G.K., Kemland, L., Anoz-Carbonell, E., Buchanan, S.K. & De Mot, R. (2017). A natural chimeric Pseudomonas bacteriocin with novel pore-forming activity parasitizes the ferrichrome transporter. MBio doi: 10.1128/mbio.01961-16. [LINK]
Noinaj, N., Gumbart, J.C. & Buchanan, S.K. (2017) The β-barrel assembly machinery in motion. Nat. Rev. Microbiol. 15:197-204.[LINK]
Bakelar, J., Buchanan, S.K. & Noinaj, N. (2017) Structural snapshots of the β-barrel assembly machinery. FEBS J. 284:1778-1786.[LINK]
Research highlighted: TTP Labtech Structural Biology newsletter, September 2019
Strickland, M., Stanley, A.M., Wang, G., Botos, I., Schwieters, C.D., Buchanan, S.K., Peterkofsky, A. & Tjandra, N. (2016). Structure of the NPr:EINNtr complex: mechanism for specificity in paralogous phophotransferase systems. Structure 24:2127-2137.[LINK]
Celia, H., Noinaj, N., Zakharov, S.D., Bordignon, E., Botos, I., Santamaria, M., Cramer, W.A., Lloubes, R. & Buchanan, S.K. (2016). Structural insight into the role of the Ton complex in energy transduction. Nature 538:60-65.[LINK]
Abeykoon, A.H., Noinaj, N., Choi, B.E., Wise, L., He, Y., Chao, C.C., Wang, G., Gucek, M., Ching, W.M., Chock, P.B., Buchanan, S.K. & Wang, D.C. (2016). Structural insights into substrate recognition and catalysis in outer membrane protein B (OmpB) by protein-lysine methyltransferases from Rickettsia. J. Biol. Chem. 291:19962-74.[LINK]
Noinaj, N., Mayclin, S. Stanley, A.M., Jao, C.C. & Buchanan, S.K. (2016). From constructs to crystals – towards structure determination of β-barrel outer membrane proteins. J. Vis. Exp. [LINK]
Botos, I., Majdalani, N., Mayclin, S.J., McCarthy, J.G., Lundquist, K., Wojtowicz, D., Barnard, T.J., Gumbart, J.C. & Buchanan, S.K. (2016). Structural and functional characterization of the LPS transporter LptDE from Gram-negative pathogens. Structure 24:965-76.[LINK]
Bakelar, J., Buchanan, S.K. & Noinaj, N. (2016). The structure of the β-barrel assembly machinery complex. Science 351:180-186.[LINK]
O’Neil, P., Rollauer, S., Noinaj, N. & Buchanan, S.K. (2015). Fitting the pieces of the beta-barrel assembly machinery complex. Biochemistry 54:6303-11.[LINK]
Kuszak, A.J., Jacobs, D., Gurnev, P.A., Shiota, T., Louis, J., Lithgow, T., Bezrukov, S.M., Rostovtseva, T.K & Buchanan, S.K. (2015). Evidence of distinct channel conformations and substrate binding affinities for the mitochondrial outer membrane protein translocase pore Tom40. J. Biol. Chem. 290:26204-17.[LINK]
Rollauer, S.E., Sooreshjani, M.A., Noinaj, N. & Buchanan, S.K. (2015). Outer membrane protein biogenesis in Gram-negative bacteria. Royal Soc. Phil. Trans. B, 370: 20150023.[LINK]
Cash, D., Noinaj, N. Buchanan, S.K. & Cornelissen, C.N. (2015). Beyond the crystal structure: insight into the function and vaccine potential of TbpA expressed by Neisseria gonorrhoeae. Infect. Immun. 83:4438-49.[LINK]
Noinaj, N., Rollauer, S.E. & Buchanan, S.K. (2015). The β-barrel membrane protein insertase machinery from Gram-negative bacteria. Curr. Opin. Struct. Biol. 31:35-24.[LINK]
Books Edited
Noinaj, N. & Buchanan, S.K., Editors (2015). The BAM Complex: Methods and Protocols. Methods in Molecular Biology Series, Humana Press, USA (Springer publishing group), ISBN 978-1-4939-2870-5 (283 pages).
Shen, H., Leyton, D.L., Shiota, T., Belousoff, M.J., Noinaj, N., Lu, J., Holt, S.A., Tan, K., Selkrig, J., Webb, C.T., Buchanan, S.K., Martin, L.L. & Lithgow, T. (2014). Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes. Nat. Commun. 5:5078.[LINK]
Noinaj, N. Kuszak, A.J., Balusek, C. Gumbart, J.C. & Buchanan, S.K. (2014). Lateral opening and exit pore formation are required for BamA function. Structure 22:1055-62.[LINK]
Yu, X., Strub, M.P., Barnard, T.J., Noinaj, N., Piszczek, G., Buchanan, S.K. & Taraska, J.W. (2014). An engineered palette of metal ion quenchable fluorescent proteins. PLoS One, 2014 Apr 21;9(4):e95808. doi: 10.1371/journal.pone.0095808. eCollection 2014. [LINK]
Noinaj, N. & Buchanan, S.K. (2014). FhaC takes a bow to FHA in the two-partner do-si-do. Mol. Microbiol. 92:1155-1158. [LINK]
Noinaj, N. & Buchanan, S.K. (2014). Structural insights into the transport of small molecules across membranes. Curr. Opin. Struct. Biol. 27:8-15.[LINK]
Noinaj, N., Kuszak, A.J., Gumbart, J.C., Lukacik, P., Chang, H., Easley, N.C., Lithgow, T. & Buchanan, S.K. (2013). Structural insight into the biogenesis of beta barrel membrane proteins. Nature 501: 385-390. [LINK]
Research highlighted: Nat. Struct. Mol. Biol. 20, 1237-1239 (2013)
Research highlighted: Faculty of 1000: F1000Prime
Research highlighted: NIDDK 2014 Annual Report
Research highlighted: MONASH Magazine
Research highlighted: Georgia Tech website
Bossermann, M.A., Downey, T. Noinaj, N., Buchanan, S.K. & Rohr, J. (2013). Molecular insight into substrate recognition and catalysis in the Baeyer-Villiger monooxygenase MtmOIV, the key frame modifying enzyme in the biosynthesis of anticancer agent mithramycin. ACS Chem. Biol. 8, 2466-2477. [LINK]
Madden, J.T., Toth, S.J., Dettmar, C.M., Newman, J.A., Oglesbee, R.A., Hedderich, H.G., Everly, R.M., Becker, M., Ronau, J.A., Buchanan, S.K., Cherezov, V., Morrow, M.E., Xu, S., Ferguson, D., Makarov, O., Das, C., Fischetti, R. & Simpson, G.J. (2013). Integrated nonlinear optical imaging microscope for on-axis crystal detection and centering at a synchrotron beamline. J. Synchrotron Radiat. 20, 531-540. [LINK]
Noinaj N, Buchanan SK, Cornelissen CN. (2012). The transferrin-iron import system from pathogenic Neisseria species. Mol Microbiol. (in press) Sep 7. doi: 10.1111/mmi.12002. [HTML] [PDF]
Webb CT, Selkrig J, Perry AJ, Noinaj N, Buchanan SK, Lithgow T. (2012). Dynamic Association of BAM Complex Modules Includes Surface Exposure of the Lipoprotein BamC. J Mol Biol. 422(4):545-55. [HTML] [PDF]
Lukacik P, Barnard TJ, Keller PW, Chaturvedi KS, Seddiki N, Fairman JW, Noinaj N, Kirby TL, Henderson JP, Steven AC, Hinnebusch BJ, & Buchanan, S.K. (2012). Structural engineering of a phage lysin that targets gram-negative pathogens. Proc Natl Acad Sci U S A. 109(25):9857-62. [HTML] [PDF]
Fairman JW, Dautin N, Wojtowicz D, Liu W, Noinaj N, Barnard TJ, Udho E, Przytycka TM, Cherezov V, & Buchanan, S.K. (2012). Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E. coli and enteropathogenic Y. pseudotuberculosis. Structure, 3;20(7):1233-43. [HTML] [PDF]
Noinaj, N., Easley, N.C., Oke, M., Mizuno, N., Gumbart, J., Boura, E., Steere, A.N., Zak, O., Aisen, P., Tajkhorshid, E., Evans, R.W., Gorringe, A.R., Mason, A.B., Steven, A.C., & Buchanan, S.K. (2012). Structural basis for iron piracy by pathogenic Neisseria. Nature (Research Article), 483 (7387):53-8. [HTML] [PDF]
Barnard TJ, Gumbart J, Peterson JH, Noinaj N, Easley NC, Dautin N, Kuszak AJ, Tajkhorshid E, Bernstein HD, & Buchanan, S.K. (2012). Molecular basis for the activation of a catalytic asparagine residue in a self-cleaving bacterial autotransporter. JMB, Jan 6;415(1):128-42. [HTML] [PDF]
Noinaj N, Wattanasak R, Lee DY, Wally JL, Piszczek G, Chock PB, Stadtman TC, & Buchanan, S.K. (2012). Structural Insights into the Catalytic Mechanism of Escherichia coli Selenophosphate Synthetase. J. Bacteriology, Jan; 194(2):499-508. [HTML] [PDF]
Hinnebusch, B.J., Jarrett, C., Callison, J., Gardner, D., Buchanan, S.K. & Plano, G. (2011). Role of the Yersinia pestis Ail Protein in Preventing a Protective Polymorphonuclear Leukocyte Response During Bubonic Plague. Infect. Immun., Dec;79(12):4984-9. [HTML] [PDF]
Yamashita, S., Lukacik, P., Barnard, T.J., Noinaj, N. Felek, S., Tsang, T.M., Krukonis, E.S., Hinnebusch, B.J. & Buchanan, S.K. (2011). Structural insights into Ail-mediated adhesion in Yersinia pestis. Structure, Nov 9;19(11):1672-82. [HTML] [PDF]
Fairman, J.W., Noinaj, N. & Buchanan, S.K. (2011). The structural biology of β-barrel membrane proteins: a summary of recent reports. Curr Opin Struct Biol. 21, 523-531. [HTML] [PDF]
Noinaj N., Bosserman M.A., Schickli M.A., Piszczek G., Kharel M.K., Pahari P., Buchanan, S.K., Rohr J. (2011). The Crystal Structure and Mechanism of an Unusual Oxidoreductase, GilR, Involved in Gilvocarcin V Biosynthesis. J Biol Chem., 286(26), 23533-43. [HTML] [PDF]
Noinaj, N., Fairman, J.W. & Buchanan, S.K. (2011). The crystal structure of BamB suggests interactions with BamA and its role within the BAM complex. J. Mol. Biol., 407, 248-260. [HTML] [PDF]
Tong, J., Dolezal, P., Selkrig, J., Crawford, S., Simpson, A.G.B., Nicholas Noinaj, N., Buchanan, S.K., Gabriel, K. & Lithgow, T. (2010). Ancestral and derived protein import pathways in the mitochondrion of Reclinomonas americana. Mol Biol Evol. 2010 Nov 15. [HTML] [PDF]
Noinaj, N., Guillier, M., Barnard, T.J. & Buchanan, S.K. (2010). TonB-dependent transporters: regulation, structure, and function. Annu Rev Microbiol. Oct 13;64:43-60. [HTML] [PDF] [ Supplemental Materials Download ]
Udho, E. Jakes, K.S., Buchanan, S.K., James, K., Jiang, X., Klebba, P.E. & Finkelstein, A. (2009). Reconstitution of bacterial outer membrane TonB-dependent transporters in planar lipid bilayer membranes. Proc. Natl. Acad. Sci. USA, 106, 21990-21995. PMCID: PMC2799797. [HTML] [PDF]
Anwari, K., Poggio, S., Perry, A., Gatsos, X., Ramarathinam, S.H., Williamson, N.A., Noinaj, N., Buchanan, S.K., Gabriel, K., Purcell, A.W., Jacobs-Wagner, C. & Lithgow, T. (2009). A modular BAM complex in the outer membrane of the model a-proteobacterium Caulobacter crescentus. PLoS One, 5(1), e8619. PMCID: PMC2797634. [HTML] [PDF]
Dagley, M.J., Dolezal, P., Likic, V.A., Smid, O., Purcell, A.W., Buchanan, S.K., Tachezy, J. & Lithgow, T. (2009). The protein import channel in the outer mitosomal membrane of Giardia intestinalis. Mol. Biol. Evol., 5(1), e8619. PMCID: PMC2797634. [HTML] [PDF]
Gatsos, X., Perry, A.J., Anwari, K., Dolezal, P., Wolynec, P.P., Likić, V.A., Purcell, A,W., Buchanan, S.K. & Lithgow, T. (2008). Protein secretion and outer membrane assembly in α-proteobacteria. FEMS Microbiol. Rev., 26, 1941-1947. PMCID: PMC2734158. [HTML] [PDF]
Brooks, B.E. & Buchanan, S.K. (2008). Signals for activation of extra cytoplasmic function (ECF) sigma factors. Biochim. Biophys. Acta: Biomembranes, 1778, 1930-1945. PMCID: PMC2562455. [HTML] [PDF]
Barnard, T.J., Dautin, N., Lukacik, P., Bernstein, H.D. & Buchanan, S.K. (2007). Autotransporter structure reveals intra-barrel cleavage followed by conformational changes. Nat. Struct. Mol. Biol 14, 1214-1220. PMCID: PMC2551741. [HTML] [PDF]
Cascales, E., Buchanan, S.K., Duché, D., Kleanthous, C., Lloubès, R., Postle, K., Riley, M.A., Slatin, S. & Cavard, D. (2007). Colicin biology. Microbiol. Mol. Biol. Rev. 71, 158-229. PMCID: PMC1847374. [HTML] [PDF]
Buchanan, S.K., Lukacik, P., Grizot, S., Ghirlando, R., Ali, M.M.U., Barnard, T.J., Jakes, K.S., Kienker, P.K. & Esser, L.(2007).Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import. EMBO J. 26, 2594-2604. PMCID: PMC1868905. [HTML] [PDF]
Wally, J & Buchanan, S.K. (2007) A structural comparison of human serum transferrin and human lactoferrin. Biometals 20, 249-262. PMCID: PMC2547852. [HTML] [PDF]
Wally, J.L., Halbrooks, P.J., Vonrhein, C., Rould, M.A., Everse, S.J., Mason, A.B. & Buchanan, S.K. (2006). The crystal structure of apo human serum transferrin provides insight into inter-lobe communication and receptor binding. J. Biol. Chem. 281, 24934-24944. PMCID: PMC1895924. [HTML] [PDF]
Buchanan, S.K. (2005). Bacterial metal detectors. Mol. Microbiol., 58, 1205-1209. PMCID: PMC1343523. [HTML] [PDF]
Schalk, I.J., Yue, W.W. & Buchanan, S.K. (2004). Recognition of iron-free siderophores by TonB-dependent iron transporters. Mol. Microbiol. 54, 14-22. [HTML] [PDF]
Oke, M., Sarra, R., Ghirlando, R., Farnaud, S., Gorringe, A.R., Evans, R.W. & Buchanan, S.K. (2004). The plug domain of a neisserial TonB-dependent transporter retains structural integrity in the absence of its transmembrane beta barrel. FEBS Lett. 564, 294-300. [HTML] [PDF]
Grizot, S. & Buchanan, S.K. (2004). Structure of the OmpA-like domain of RmpM from Neisseria meningitidis. Mol. Microbiol. 51, 1027-1037. [HTML] [PDF]
Yue, W.W., Grizot, S. & Buchanan, S.K. (2003). Structural evidence for iron-free citrate and ferric citrate binding to the TonB-dependent outer membrane transporter FecA. J. Mol. Biol. 332, 353-368. [HTML] [PDF]
Oakhill, J.S., Joannou, C.L., Buchanan, S.K., Gorringe, A.R. & Evans, R.W. (2002). Expression and purification of functional recombinant meningococcal transferrin-binding protein A. Biochem. J., 364, 613-616. PMCID: PMC1222609. [HTML] [PDF]
Gabriel, K., Buchanan, S.K. & Lithgow, T. (2001). The alpha and the beta: protein translocation across outer membranes. Trends Biochem. Sci. 26, 36-40. [HTML] [PDF]
Buchanan, S.K. (2001). Type I secretion and multidrug efflux: transport through the TolC channel-tunnel. Trends Biochem. Sci. 26, 3-6. [HTML] [PDF]
Istvan, E.S., Palnitkar, M., Buchanan, S.K. & Deisenhofer, J. (2000). Crystal
structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis. EMBO J. 19, 819-830. PMCID: PMC305622. [HTML] [PDF]
Buchanan, S.K. (1999). Overexpression and refolding of an 80 kDa iron transporter from the outer membrane of Escherichia coli. Biochem. Soc. Trans. 27, 903-908. [HTML] [PDF]
Buchanan, S.K. (1999). Beta-barrel proteins from bacterial outer membranes: structure, function and refolding. Curr. Opin. Struct. Biol. 9, 455-461. [HTML] [PDF]
Buchanan, S.K., Smith, B.S., Venkatramani, L., Xia, D., Palnitkar, M., Chakraborty, R., van der Helm, D. & Deisenhofer, J. (1999). Crystal structure of the outer membrane active transporter FepA from Escherichia coli. Nat. Struct. Biol. 6, 56-63. [HTML] [PDF]
Smith, B.S., Kobe, B., Kurumbail, R., Buchanan, S.K., Venkatramani, L., van der Helm, D. & Deisenhofer, J. (1998). Crystallization and preliminary X-ray analysis of ferric enterobactin receptor FepA, an integral membrane protein from E. coli. Acta Crystallogr.D54, 697-699. [HTML] [PDF]
Abrahams, J.P., Buchanan, S.K., van Raaij, M.J., Fearnley, I.M., Leslie, A.G.W. & Walker, J.E. (1996). The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin. Proc. Natl. Acad. Sci. USA, 93, 9320-9424. PMCID: PMC38443. [HTML] [PDF]
Buchanan, S.K. & Walker, J.E. (1996). Large scale chromatographic purification of F1Fo-ATPase and complex I from bovine heart mitochondria. Biochem. J. 318, 343-349. PMCID: PMC1217627. [HTML] [PDF]
Collinson, I.R., Runswick, M.J., Buchanan, S.K., Fearnley, I.M., Skehel, M.J., van Raaij, M.J., Griffiths, D.E. & Walker, J.E. (1994). Fo membrane domain of ATP synthase from bovine heart mitochondria: purification, subunit composition, and reconstitution with F1-ATPase. Biochemistry 33, 7971-7978. [HTML] [PDF]
Ermler, U., Fritzsch, G., Buchanan, S.K. & Michel, H. (1994). Structure of the photosynthetic reaction center from Rhodobacter sphaeroides at 2.65 Å resolution: cofactors and protein-cofactor interactions. Structure 2, 925-936. [HTML] [PDF]
Lutter, R., Abrahams, J.P., van Raaij, M., Todd, R.J., Lundquist, T., Buchanan, S.K., Leslie, A. & Walker, J.E. (1993). Crystallization of F1-ATPase from bovine heart mitochondria. J. Mol. Biol. 229, 787-790. [HTML] [PDF]
Buchanan, S.K., Fritzsch, G., Ermler, U. & Michel, H. (1993). A new crystal form of the photosynthetic reaction centre from Rhodobacter sphaeroides of improved diffraction quality. J. Mol. Biol. 230, 1311-1314. [HTML] [PDF]
Buchanan, S., Michel, H. & Gerwert, K. (1992). Light-induced charge separation in Rhodopseudomonas viridis reaction centers monitored by Fourier-transform infrared difference spectroscopy: the quinone vibrations. Biochemistry 31, 1314-1322. [HTML] [PDF]
Dressler, K., Umlauf, E., Schmidt, S., Hamm, P., Zinth, W., Buchanan, S. & Michel, H. (1991). Detailed studies of the subpicosecond kinetics in the primary electron transfer of reaction centers of Rhodopseudomonas viridis. Chem. Phys. Lett. 183, 270-276. [HTML] [PDF]
Fritzsch, G., Buchanan, S. & Michel, H. (1989). Assignment of cytochrome hemes in crystallized reaction centers from Rhodopseudomonas viridis. Biochim. Biophys. Acta 977, 157-162. [HTML] [PDF]
Gerwert, K., Hess, B., Michel, H. & Buchanan, S. (1988). FTIR studies on crystals of photosynthetic reaction centers. FEBS Lett. 232, 2, 303-307. [HTML] [PDF]
Buchanan, S.K., Dismukes, G.C. & Prince, R.C. (1988). The redox potential of the primary quinone QA of bacterial photosynthesis is independent of the divalent metal ion. FEBS Lett. 229, 1, 16-20. [HTML] [PDF]
Buchanan, S.K. & Dismukes, G.C. (1987). Substitution of Cu2+ in the reaction center diquinone electron acceptor complex of Rhodobacter sphaeroides: determination of the metal-ligand coordination. Biochemistry 26, 5049-5055. [HTML] [PDF]
Buchanan, S., Kubler, D.G., Meigs, C., Owens, M. & Talman, A. (1983). Energy of activation and temperature for the hydrolysis of sucrose. Intl. J. Chem. Kinetics 15, 11, 1229-1234. [ABSTRACT]
Fleming, K.G., Yamashita, S. & Buchanan, S.K. (2010). Structure and folding of outer membrane proteins. In Comprehensive Biophysics, Volume V: Membranes, Elsevier Science Ltd., in press.
Yamashita, S. & Buchanan, S.K. (2010). Solute and ion transport: outer membrane pores and receptors. In A. Böck, R. Curtiss III, J. B. Kaper, P. D. Karp, F. C. Neidhardt, T. Nyström, J. M. Slauch, and C. L. Squires, and D. Ussery (ed.), EcoSal - Escherichia coli and Salmonella: cellular and molecular biology. https://www.ecosal.org. ASM Press, Washington, DC. doi: 10.1128/ecosal.3.3.1. [LINK]
Barnard, T.J., Wally, J.L. & Buchanan, S.K. (2006). Crystallization of integral membrane proteins. In Current Protocols in Protein Science 17.9, 1-15, John Wiley & Sons, Inc. (DOI: 10.1002/0471140864.ps1709s47). [HTML] [PDF]
Walker, J.E., Skehel, M.J. & Buchanan, S.K. (1995). Structural analysis of NADH-
ubiquinone oxidoreductase from bovine heart mitochondria. Meth. Enzymol. 260, 14-34. [PDF]
Buchanan, S.K. & Walker, J.E. (1993). Chromatographic purification of F1Fo-ATPase and complex I from bovine heart mitochondria. In A Practical Guide to Membrane Protein Purification (von Jagow, G. & Schägger, H., eds.), Academic Press, San Diego, 125-133. [LINK]
Buchanan, S., Michel, H. & Gerwert, K. (1990). Investigation of quinone reduction in Rps. viridis by FTIR difference spectroscopy and x-ray diffraction analysis. In Springer Series in Biophysics: Reaction centers of Photosynthetic bacteria (Michel-Beyerle, M. E., ed.) Springer Verlag, Berlin, 6, 75-85. [LINK]
Buchanan, S., Michel, H., Hess, B. & Gerwert, K. (1990). FTIR studies of light-induced intramolecular processes on crystals and reconstituted reaction centers from Rhodopseudomonas viridis. In Current Research in Photosynthesis (Baltscheffsky, M., ed.), Kluwer Academic Publishers, Dordrecht, I, 69-72. [LINK]
Grisshammer, R & Buchanan, S.K., Editors (2006). Structural Biology of Membrane Proteins, Royal Society of Chemistry Biomolecular Sciences Series, Cambridge, RSC Publishing, ISBN 0-85404-361-6 (392 pages). [LINK]