Professional Information
B.S., Bowling
Green State University, 1979
Ph.D., University
of Illinois at Urbana-Champaign,
1987
NSF Postdoctoral Fellow, University of California at San Diego, 1987-1989
LANL Postdoctoral Director's Fellow, Los Alamos National Laboratory, 1989-1991
Research Interests:
Infrared Spectroscopic Studies of
Metalloproteins.
Research efforts in my laboratory center on
using infrared spectroscopy to examine the
roles that the cofactors and active site amino acids play in the function
of metalloenzymes. We are currently using infrared spectroscopy to
study the structure and function of two classes of
metalloproteins:
1) The Hydrogenases catalyze the reversible oxidation of molecular hydrogen (H2).
Three forms of hydrogenases are known which differ in their active site
structure.
a) In the [NiFe] hydrogenases, the active site contains a Ni
ion that is bridged to an Fe(CN)2CO
moiety by two conserved
cysteine residues.
b)
The active site of the [FeFe] Hydrogenases (also
known as Fe-only
hydrogenases) consists of a 2Fe subcluster in which
two Fe(CO)(CN) moieties are bridged by a CO ligand and a
dithiol (S-X-S) moeity of unknown composition. The 2Fe subcluster
is tethered to the the protein by a thiolate from conserved cystiene
which bridges between the 2Fe subcluster and a nearby 4Fe-4S
cluster.
c) The active site of the FeS cluster free hydrogenase
(5,10-methenyltetrahydromethanopterin hydrogenase or Hmd) contains a Fe(CO)2
moiety at its active site.
Our current research efforts on the hydrogenase project
include: 1) Utilizing infrared signatures in the
2100-1800 cm-1
spectral region that from the intrinsic metal coordinated carbon
monoxide and cyanide ligands, which are unique to this class of
enzymes. This
approach provides a unique opportunity since the
frequencies of the IR bands associated with the CO and CN ligands
at the active site of these enzymes are extremely sensitive to
the redox and coordination environment of the metals at the
active site; 2) Extension of our infrared studies into the
mid-infrared spectral region (2000-700
cm-1);
Mid-infrared difference
spectroscopy allows us to examine the role
conserved amino acids play in the activation of hydrogen by these
enzymes. Over the years we have collaborated with researchers
from around the world on various aspects of this project (e.g. England,
France, Germany, Japan, The Netherlands, and the USA).
2) The Carbon Monoxide Deydrogenase/ Acetyl-CoA
synthase (CODH/ACS) is a bifunctional enzyme that catalyzes the
reversible reduction of carbon dioxide into carbon monoxide, and, the
coupled synthesis of acetyl-CoA from the carbon monoxide produced by the CODH domain of the enzyme.
This reaction is an important component of 1-C metabolic
processes in a number of microrganisms that are capable of growth on
one carbon sources. In
collaboration with Dr. Stephen Ragsdale,
Department of Biological Chemistry, University at Michigan, we have used IR spectroscopy to study
CODH/ACS from Moorella thermoacetica after incubation under CO. Our results show that carbon monoxide binds
in a terminal fashion to metal ions at the active sites of both CODH
and ACS in this complex. Additionally, our IR
studies show that the CODH active site is capable of oxidizing CO into CO2 at the CODH active site in the absence of an added electron acceptor.
Infrared Spectroscopic Studies of Metastable State Linkage Isomers:
Transition metal complexes of the type ML5(NO). xH2O
have a ground state stucture in which NO is coordinated to the metal
via the nitrogen (M-NO). Upon irradiation with UV-visible light at
low temperatures, two species are formed which differ in how the
NO is coordinated to the metal center. One of these metastable states (termed MS I)
has been shown to be an oxygen bound isonitrosyl (M-ON),
while the other (MS II) has been shown to be a side
bound NO. FTIR spectroscopy in parallel with x-ray
photocrystallography, differential scanning calorimetry, and density
functional calculations have been instrumental in the study of these
systems. In collaboration with Dr. Philip Coppens,
Department of Chemistry, SUNY at Buffalo, and Dr. George Richter-Addo,
Department of Chemistry and Biochemistry, University of Oklahoma,
we have shown that the
formation of metastable state linkage isomers is seen not only in
simple transition metal nitrosyls of the type described above,
but also occurs in Ru and Fe porphyrin nitrosyls.
Additionally, the formation of linkage isomers is not
limited to NO complexes. A side bound dinitrogen is formed upon
irradiation of Os(NH3)5(N2)2+; In Ru
sulfur dioxide complexes side bound and O-bound isomers of the sulfur dioxide have been detected, and, in Fe(NO)(NO2) complexes double linkage isomers involving both NO and NO2 are found.
Time Resolved Infrared Spectroscopy:
A new FTIR spectrometer (Bruker IFS66v/s) and a pulsed II NdYAG laser (Continuum Surelite II) suitable
for collecting IR spectra as a function of time following an event
triggered by a laser have recently been installed at Buffalo
State. Funding for the project was provided by the National
Science Foundation's MRI program, through a grant made to Dr. Philip Coppens (University at Buffalo) and me. This system allows for collection of mid- IR
spectra following a laser flash in the either rapid scan or step scan
mode of the FTIR. A 200 MHz digitization board coupled to a
photovoltaic MCT detector in the FTIR allows for the collection of time
resolved infared data in the step scan mode with a time resolution of up to 10 ns.
Publications:
32. Characterization
of a Cyanobacterial-like Uptake [NiFe]-Hydrogenase. EPR and FTIR Spectroscopic Studies of the Enzyme from Acidithiobacillus ferrooxidans
; O. Schröder, W., B. Bleijlevens, T. de Jonge, Z. Chen, T. Li,
J. Fischer, J. Förster, C. G. Friedrich, K. A. Bagley, S. P. J.
Albracht, and W. Lubitz, J. Bioinorganic Chem. 12(2); 212-233 (2007).
[Epub 2006 -Nov. 3].
31. Experimental and Density Functional Theoretical Investigations of Linkage Isomerism in Six Coordinate {FeNO}6 Iron Porphyrins with Axial Nitrosyl and Nitro Ligands; I. V. Novozhilova, P. Coppens, J. Lee, G. B. Richter-Addo, and K. A. Bagley, J. Am. Chem. Soc. 128(6); 2093-2104 (2006).
30. Photo-induced Oxygen Transfer and Double Linkage Isomerism in a cis (NO)(NO2) Transition Metal Complex by Photocrystallography, FT-IR Spectroscopy, and DFT Calculations; A. Y Kovalevsky, G. King, K. A. Bagley, and P. Coppens, Chem. Eur. J. 11; 1-12 (2005).
29. Single and Double Linkage Isomerism in a Six-Coordinate Iron Porphyrin Containing Nitrosyl and Nitro Ligands;
J. Lee, A. Yu. Kovalevsky, I. V. Novozhilova, K. A.
Bagley, P. Coppens, and G. B. Richter-Addo; J. Am. Chem. Soc.,
(Communication) 126(23); 7180-7181(2004).
28. Infrared Studies of Carbon Monoxide Binding to Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase from Moorella thermoacetica; J.
Chen, S. Huang, J. Seravalli, H. Gutzman Jr., D. J.
Swartz, S. A. Ragsdale, and K. A. Bagley; Biochemistry 42;
14822-14830 (2003).
27. Light-Induced Metastable Linkage Isomers of Ruthenium Sulfur Dioxide Complexes; A. Y Kovalevsky , K. A. Bagley , J. M. Cole, & P. Coppens; Inorg. Chem. 42(1); 140-147 (2003).
26. The First Crystallographic Evidence for Light-Induced Metastable Linkage Isomers of Ruthenium Sulfur Dioxide Complexes; A. Y. Kovalevsky, K. A. Bagley, & P. Coppens; J. Am. Chem. Soc. 124(31); 9241-9248 (2002).
25. Infrared Studies of the CO Inhibited Form of the Fe-only Hydrogenase from Clostridium pasteurianum I: Examination of Its Light Sensitivity at Cryogenic Temperatures;
Z. Chen, B. Lemon, S. Huang, Derrick Swartz; J. W. Peters, and K. A.
Bagley; Biochemistry 41(6), 2036-2043 (2002).
24. On the Photochemical Behavior of the [Ru(NO)(NH3)4 nicotinamide]3+ cation and the Relative Stability of Light-Induced Metastable Isonitrosyl Isomers of Ru Complexes; C. Kim., I. Novozhilova, M. S. Goodman, K. A. Bagley, and P. Coppens, Inorg. Chem. 39(25), 5791-5795 (2000).
23. First Observation of Photo-induced Nitrosyl Linkage Isomers of Iron Nitrosyl Porphyrins;
L. Cheng, I. Novozhilova, C. Kim, D. Fomitchev, K. A.
Bagley, P. Coppens, and G. B. Richter-Addo, J.
Am. Chem. Soc. (Communication) 122(29), 7142-7143 (2000).
22. The First Crystallographic Evidence for Side-On Coordination of N2 to a Single Metal Center in a Photoinduced Metastable State;
D. V. Fomitchev, K. A. Bagley, and P. Coppens;
J. Am. Chem. Soc. (Communication) 122(3), 532-533 (2000).
21. Photo-induced
Metastable Linkage Isomers of
Ruthenium Nitrosyl Porphyrins; D. Fomitchev,
P. Coppens, T. Li, K. A. Bagley, L. Chen, and G. B.
Richter-Addo; Chem. Comm. 19, 2013-2014 (1999).
20. Evidence for Carbon-Monoxide and Cyanide as Intrinsic Ligands to Iron in the Active Site of [NiFe]-Hydrogenases: NiFe(CN)2CO, Biology's Way to Activate H2; A.
J. Pierik, W. Roseboom, R. P. Happe, K. A. Bagley, and S. P. J.
Albracht; J. Biol. Chem. 274 (6), 3331-3337 (1999).
19. Biological Activation of Hydrogen;
R. P. Happe, W. Roseboom, A. J. Pierik,
S. P. J. Albracht, and K. A.
Bagley; Nature 385, 126 (1997).
18. Similarities
in Architecture of the Active Sites of Ni- Hydrogenases and Fe-
Hydrogenases as Detected by Means of Infrared Spectroscopy;
T. M. Van der Speck, A. F. Arendsen, R. P. Happe, S. Yun,
K. A. Bagley, D. J. Stufkens, W. R. Hagen,
and S. P. J. Albracht, Eur. J. Biochem. 237 (3),
629-634 (1996).
17. An Infrared-Detectable Group Senses Changes in Charge Density on the Nickel Center in Hydrogenase from Chromatium vinosum; K. A. Bagley, E. C. Duin, W. Roseboom, S. P. J. Albracht, and W. H. Woodruff, Biochemistry 34(16), 5527-5535 (1995).
16. Infrared Studies on the Interaction of Carbon Monoxide With Divalent Nickel in Hydrogenase From Chromatium vinosum
; K. A. Bagley, C. Van Garderen, M. Chen, E. C.
Duin, S. P. J. Albracht, W. H. Woodruff, Biochemistry 33(31),
9229-9236 (1994).
15. An Unknown Redox Component in Nickel Hydrogenases;
S. P. J. Albracht, J. W. Van der Zwaan, M. Chen, M. H. Kolk, E. C.
Duin, K. A. Bagley, and W. H. Woodruff, Biol. Chem. Hoppe-Seyler
374, 824 (1994).
14. Ultrafast and Not-So-Fast Dynamics of Cytochrome Oxidase: The Ligand Shuttle and Its Possible Functional Significance;
W. H. Woodruff, R. B. Dyer, O. Einarsdóttir, K. A. Peterson, P.
O.Stoutland, K. A. Bagley, G. Palmer, J. R. Schoonover, D. S. Kliger,
R. A. Goldbeck, T. D. Dawes, J. -L. Martin, J .-C. Lambry, S. J.
Atherton, and S. M. Hubig; Proceedings of SPIE 1432 (Biomolecular
Spectroscopy II), 205-210, (1991).
13. The "Ligand Shuttle" Reactions of Cytochrome Oxidase: Spectroscopic Evidence, Dynamics, and Functional Significance;
W. H. Woodruff, R. B. Dyer, O. Einarsdóttir, K. A.
Peterson, P. O. Stoutland, K .A. Bagley, G. Palmer, J. R. Schoonover, D
.S. Kliger, R .A. Goldbeck, T .D. Dawes, J. -L. Martin, J. -C. Lambry,
S. J. Atherton, and S. M. Hubig; in Spectroscopy of Biological
Molecules 94 (Hester, R.E. and Girling, R.B., eds.), The Royal Society
of Chemistry, London, 235-238, (1991).
12. The
Nature and Functional Implications of the Cytochrome a3 Transients
Following Photodissociation of Carbon Monoxide from Reduced
CO-Cytochrome Oxidase; W. H. Woodruff, O. Einarsdóttir, R. B.
Dyer, K. A. Bagley, G. Palmer, S.J. Atherton, R.A. Goldbeck, T.D.
Dawes, and D.S. Kliger; Proc. Nat'l Acad. Sci. USA 88, 2588-2592 (1991).
11. Steady-State and Time-Resoved FTIR Spectroscopy of Quinones in Bacterial Reaction Centers;
D.L. Thibodeau, J. Breton, C. Berthomeau, K. A. Bagley, W. Mäntele, and
E. Nabedryk; in Reaction Centers of Photosynthetic Bacteria
(Michele-Byerle, M.E., Ed.) Springer-Verlag Series in Biophysics, Vol.
6, 87-98, (1991).
10. A Protein
Conformational Change Associated with the Photoreduction of the Primary
and Secondary Quinones in the Bactrial Reaction Center; E. Nabedryk, K. A. Bagley, D. L. Thibodeau, M. Bausher, W. Mäntele, and J. Breton; FEBS Letts. 266(1-2), 59-62 (1990).
9. Investigation of Models for Photosynthetic Electron Acceptors: Infrared Spectroelectrochemistry of Ubiquinone and its Anions; M. Bausher, E. Nabedryk, K. Bagley, J. Breton, and W. Mäntele; FEBS Letts. 261, 191-195 (1990).
8. Models
For Ubiquinones and Their Anions, Involved in the Photosynthetic
Electron Transfer, Characterized by Thin-layer Electrochemistry and
FTIR/UV-Vis Spectroscopy; M. Bauscher, K. Bagley, E. Nabedryk,
J. Breton, W. Mäntele; in Current Research in Photosynthesis, Volume I:
Proceedings of the VIIIth International Congress on Photosynthesis,
August '89 (M. Baltcheffsky, ed.) Kluwer Academic Publishers,
Dordrecht; 81-84 (1990).
7. FTIR Studies of the D+QA- and D+QB- States in Reaction Centers from Rb. Sphaeroides;
K. A. Bagley, E. Abresch, M.Y. Okamura, G. Feher, M. Bauscher, W.
Mäntele, E. Nabedryk, and J. Breton; in Current Research in
Photosynthesis, Volume I: Proceedings of the VIIIth International
Congress on Photo¬synthesis, August '89 (M. Baltcheffsky, ed.) Kluwer
Academic Publishers, Dordrecht; 77-80 (1990).
6. A
Comparitive Study of the Infrared Difference Spectra for Octopus and
Bovine Rhodopsin and Their Bathorhodopsin Photointermediates; K.A. Bagley, L. Eisenstein, T. G. Ebrey, and M. Tsuda; Biochemisry 28, 3366-3373 (1989).
5. Infrared Studies of Bovine Rhodopsin and its Low Temperature Photointermediates, Bathorhodopsin and Isorhodopsin;
K. A. Bagley, L. Eisenstein, W.-D. Ding, and K. Nakanishi, in
Biophysical Studies of Retinal Proteins (T. Ebrey, H. Frauenfenlder, B.
Honig, K. Nakanishi, eds.) University of Illinois Press, Urbana,
Illinois; 110-119 (1987).
4. Fourier-Transform Infrared Difference Spectroscopy of Rhodopsin and its Photoproducts at Low Temperatures;
K. A. Bagley, V. Balogh-Nair, A. Croteau, G. Dollinger, T. G. Ebrey, L.
Eisenstein, M. Hong, K. Nakanishi, and J. Vittitow; Biochemistry
24(22), 6055-6071 (1985).
3. Trans/ 13-cis Isomerization is Essential for Both the Photocycle and Proton Pumping of Bacteriorhodopsin;
C. H. Chang, R. Govindjee, T. Ebrey, K. Bagley, G. Dollinger, L.
Eisenstein, J. Marque, H. Roder, J. Vittitow, J. Fang, and K.Nakanishi;
Biophys. J. 47 (4), 509-512 (1985).
2. Infrared Studies of the Photocycle of Bacteriorhodopsin;
K. Bagley, G. Dollinger, L. Eisenstein, M. Hong, J. Vittitow, and L.
Zimanyi; in Information and Energy Transduction in Biological
Membranes ( E. Helmreich, ed.) Plenum Press, New York, 27-37, (1984).
1. Fourier Transform Infrared Difference Spectroscopy of Bacteriorhodopsin and its Photoproducts; K. Bagley, G. Dollinger, L. Eisenstein, A. K. Singh, and L. Zimanyi; Proc. Natl. Acad. Sci., USA 79, 4972-4976 (1982).
Science and Mathematics Complex:
I
am currently serving as the project shepherd for Buffalo State's
Science
and Mathematics Complex construction project. This 220,000 square
foot,
$100 million project includes the construction of new laboratory
wing, which is linked to our current science building via a central
atrium that places science on display via windows into the
instructional laboratories. The second phase of the project
includes the
complete renovation of the remaining portions of BSC's current
Science Building as well as the construction of new lecture halls, a
planetarium, vivarium, and greenhouse. Further information
concerning the
project can be found at the Science Building Advocacy Committee's web site.
Postbaccalaureate Teacher Certification:
I
am the academic advisor for students in the
Chemistry Department's postbaccalaureate teacher certification
program. This program provides an avenue for those individuals
who hold a chemistry or chemistry related baccalaureate degree to
obtain the required qualifications to teach in New York State's high
schools and middle schools. Individuals wishing to teach
chemistry at the high school level or general science in grades 7-8,
are served by the department's Chemistry Education (7-12; Certification Only)
program. For those individual's wishing to be certified to teach
science in grades 5-6 as well, we offer an extension to our 7-12
program called the Chemistry Education (7-12; 5-6 Extension; Certification Only)
program. Individuals in both programs are placed for student
teaching in the final semster of the program. While completing these
programs, students have two academic advisors; I advise on all
matters
related to their required chemistry coursework, while Dr. Joseph Zawicki ,
Department of Earth Science and Science Education, acts as the
advisor for all matters related to the education coursework.
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