FIND

researchers

DISCOVER

relevant articles

PROMOTE

your research

now for free

Joann Sanders-Loehr

Research Profile

Phenomena

Chemicals & Drugs

Concepts & Ideas

Occupations

Spectrum Analysis

Living Beings

Escherichia coli

Co-author Network

Publications

TOP 3
Frederik J Rotsaert; Jeremie D Pikus; Brian G Fox; John Lute Markley; Joann Sanders-Loehr
N-isotope effects on the Raman spectra of Fe(2)S(2) ferredoxin and Rieske ferredoxin: evidence for structural rigidity of metal sites.
Irene M C van Amsterdam; Marcellus Ubbink; Marieke van den Bosch; Frederik Rotsaert; Joann Sanders-Loehr; Gerard W Canters
A new type 2 copper cysteinate azurin. Involvement of an engineered exposed cysteine in copper binding through internal rearrangement.
Edward L Green; Nobuhumi Nakamura; David M Dooley; Judith P Klinman; Joann Sanders-Loehr
Rates of oxygen and hydrogen exchange as indicators of TPQ cofactor orientation in amine oxidases.

Register for free to view:

Visualized networks:

See your personal network in
sophisticated graphical views

GeoTargeted Searches:

Locate experts around the world
and connect with global collaborators

Research Profiles:

See the research activity
of experts around the globe

Geonetwork of Joann Sanders-Loehr (preview)

Cities where this author has publications
Cities where co-authors of this author have publications

Flash Player Required

All Publications

2003: Frederik J Rotsaert; Jeremie D Pikus; Brian G Fox; John Lute Markley; Joann Sanders-Loehr
N-isotope effects on the Raman spectra of Fe(2)S(2) ferredoxin and Rieske ferredoxin: evidence for structural rigidity of metal sites.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 2003;8(3):318-26.
2002: Irene M C van Amsterdam; Marcellus Ubbink; Marieke van den Bosch; Frederik Rotsaert; Joann Sanders-Loehr; Gerard W Canters
A new type 2 copper cysteinate azurin. Involvement of an engineered exposed cysteine in copper binding through internal rearrangement.
The Journal of biological chemistry 2002;277(46):44121-30.
2002: Edward L Green; Nobuhumi Nakamura; David M Dooley; Judith P Klinman; Joann Sanders-Loehr
Rates of oxygen and hydrogen exchange as indicators of TPQ cofactor orientation in amine oxidases.
Biochemistry 2002;41(2):687-96.
2001: C S Farmer; Donald M Kurtz; Z J Liu; Bi-Cheng Wang; J Rose; Jingyuan Ai; Joann Sanders-Loehr
The crystal structures of Phascolopsis gouldii wild type and L98Y methemerythrins: structural and functional alterations of the O2 binding pocket.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 2001;6(4):418-29.
2001: Marcela L Alvarez; J Ai; Walter G Zumft; Joann Sanders-Loehr; David M Dooley
Characterization of the copper-sulfur chromophores in nitrous oxide reductase by resonance raman spectroscopy: evidence for sulfur coordination in the catalytic cluster.
Journal of the American Chemical Society 2001;123(4):576-87.
2000: Tim Rasmussen; Ben C Berks; Joann Sanders-Loehr; David M Dooley; Walter G Zumft; Andrew J Thomson
The catalytic center in nitrous oxide reductase, CuZ, is a copper-sulfide cluster.
Biochemistry 2000;39(42):12753-6.
2000: Karen S Lyle; P Möenne-Loccoz; Jingyuan Ai; Joann Sanders-Loehr; Thomas M Loehr; Brian G Fox
Resonance Raman studies of the stoichiometric catalytic turnover of a substrate-stearoyl-acyl carrier protein delta(9) desaturase complex.
Biochemistry 2000;39(34):10507-13.
2000: J Xiong; Robert S Phillips; Donald M Kurtz; S Jin; Jingyuan Ai; Joann Sanders-Loehr
The O(2) binding pocket of myohemerythrin: role of a conserved leucine.
Biochemistry 2000;39(29):8526-36.
2000: H Liu; Haining Zhu; Daryl K Eggers; Aram M Nersissian; Kym F Faull; JJ Goto; Jingyuan Ai; Joann Sanders-Loehr; Edith Butler Gralla; Joan Selverstone Valentine
Copper(2+) binding to the surface residue cysteine 111 of His46Arg human copper-zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant.
Biochemistry 2000;39(28):8125-32.
2000: C R Melville; Edward L Green; Joann Sanders-Loehr; Judith P Klinman
Reassessment of the active site quino-cofactor proposed to occur in the Aspergillus niger amine oxidase AO-I from the properties of model compounds.
Biochemistry 2000;39(25):7589-94.
2000: C S Farmer; Donald M Kurtz; Robert S Phillips; Jingyuan Ai; Joann Sanders-Loehr
A leucine residue "Gates" solvent but not O2 access to the binding pocket of phascolopsis gouldii hemerythrin.
The Journal of biological chemistry 2000;275(22):17043-50.
2000: J Xiong; Donald M Kurtz; Jingyuan Ai; Joann Sanders-Loehr
A hemerythrin-like domain in a bacterial chemotaxis protein.
Biochemistry 2000;39(17):5117-25.
1999: J Plastino; Edward L Green; Joann Sanders-Loehr; Judith P Klinman
An unexpected role for the active site base in cofactor orientation and flexibility in the copper amine oxidase from Hansenula polymorpha.
Biochemistry 1999;38(26):8204-16.
1998: B Schwartz; Edward L Green; Joann Sanders-Loehr; Judith P Klinman
Relationship between conserved consensus site residues and the productive conformation for the TPQ cofactor in a copper-containing amine oxidase from yeast.
Biochemistry 1998;37(47):16591-600.
1998: John A Broadwater; Jingyuan Ai; Thomas M Loehr; Joann Sanders-Loehr; Brian G Fox
Peroxodiferric intermediate of stearoyl-acyl carrier protein delta 9 desaturase: oxidase reactivity during single turnover and implications for the mechanism of desaturation.
Biochemistry 1998;37(42):14664-71.
1998: Albrecht Messerschmidt; L Prade; SJ Kroes; Joann Sanders-Loehr; Robert Huber; Gerard W Canters
Rack-induced metal binding vs. flexibility: Met121His azurin crystal structures at different pH.
Proceedings of the National Academy of Sciences of the United States of America 1998;95(7):3443-8.
1997: S X Wang; N Nakamura; Minae Mure; Judith P Klinman; Joann Sanders-Loehr
Characterization of the native lysine tyrosylquinone cofactor in lysyl oxidase by Raman spectroscopy.
The Journal of biological chemistry 1997;272(46):28841-4.
1997: N Nakamura; Pierre Moanne-Loccoz; Katsuyuki Tanizawa; Minae Mure; Shinnichiro Suzuki; Judith P Klinman; Joann Sanders-Loehr
Topaquinone-dependent amine oxidases: identification of reaction intermediates by Raman spectroscopy.
Biochemistry 1997;36(38):11479-86.
1997: D Cai; JE Dove; N Nakamura; Joann Sanders-Loehr; Judith P Klinman
Mechanism-based inactivation of a yeast methylamine oxidase mutant: implications for the functional role of the consensus sequence surrounding topaquinone.
Biochemistry 1997;36(38):11472-8.
1996: SJ Kroes; C W Hoitink; C R Andrew; J Ai; Joann Sanders-Loehr; Albrecht Messerschmidt; W R Hagen; Gerard W Canters
The mutation Met121-->His creates a type-1.5 copper site in Alcaligenes denitrificans azurin.
European journal of biochemistry / FEBS 1996;240(2):342-51.
1996: Pierre Moanne-Loccoz; N Nakamura; S Itoh; S Fukuzumi; A C Gorren; Johannis A Duine; Joann Sanders-Loehr
Electrostatic environment of the tryptophylquinone cofactor in methylamine dehydrogenase: evidence from resonance Raman spectroscopy of model compounds.
Biochemistry 1996;35(15):4713-20.
1996: N Nakamura; R Matsuzaki; Y H Choi; K Tanizawa; Joann Sanders-Loehr
Biosynthesis of topa quinone cofactor in bacterial amine oxidases. Solvent origin of C-2 oxygen determined by Raman spectroscopy.
The Journal of biological chemistry 1996;271(9):4718-24.
1996: Gertie van Pouderoyen; C R Andrew; Thomas M Loehr; Joann Sanders-Loehr; S Mazumdar; H Allen O Hill; Gerard W Canters
Spectroscopic and mechanistic studies of type-1 and type-2 copper sites in Pseudomonas aeruginosa azurin as obtained by addition of external ligands to mutant His46Gly.
Biochemistry 1996;35(5):1397-407.
1995: A C Gorren; P Moenne-Loccoz; G Backes; Simon de Vries; Joann Sanders-Loehr; Johannis A Duine
Evidence for a methylammonium-binding site on methylamine dehydrogenase of Thiobacillus versutus.
Biochemistry 1995;34(40):12926-31.
1995: Pierre Moanne-Loccoz; N Nakamura; V Steinebach; Johannis A Duine; Minae Mure; Judith P Klinman; Joann Sanders-Loehr
Characterization of the topa quinone cofactor in amine oxidase from Escherichia coli by resonance Raman spectroscopy.
Biochemistry 1995;34(21):7020-6.
1994: Brian G Fox; John Shanklin; J Ai; Thomas M Loehr; Joann Sanders-Loehr
Resonance Raman evidence for an Fe-O-Fe center in stearoyl-ACP desaturase. Primary sequence identity with other diiron-oxo proteins.
Biochemistry 1994;33(43):12776-86.
1994: J Ling; Margareta Sahlin; Britt-Marie Sjöberg; Thomas M Loehr; Joann Sanders-Loehr
Dioxygen is the source of the mu-oxo bridge in iron ribonucleotide reductase.
The Journal of biological chemistry 1994;269(8):5595-601.
1993: T den Blaauwen; C W Hoitink; Gerard W Canters; J Han; Thomas M Loehr; Joann Sanders-Loehr
Resonance Raman spectroscopy of the azurin His117Gly mutant. Interconversion of type 1 and type 2 copper sites through exogenous ligands.
Biochemistry 1993;32(46):12455-64.
1993: M Van de Kamp; Gerard W Canters; C R Andrew; Joann Sanders-Loehr; C J Bender; Jack Peisach
Effect of lysine ionization on the structure and electrochemical behaviour of the Met44-->Lys mutant of the blue-copper protein azurin from Pseudomonas aeruginosa.
European journal of biochemistry / FEBS 1993;218(1):229-38.
1993: Thomas M Loehr; Joann Sanders-Loehr
Techniques for obtaining resonance Raman spectra of metalloproteins.
Methods in enzymology 1993;226():431-70.
1992: M Ormö; F deMaré; K Regnström; A Aberg; Margareta Sahlin; J Ling; Thomas M Loehr; Joann Sanders-Loehr; Britt-Marie Sjöberg
Engineering of the iron site in ribonucleotide reductase to a self-hydroxylating monooxygenase.
The Journal of biological chemistry 1992;267(13):8711-4.
1992: M L Howell; Joann Sanders-Loehr; Thomas M Loehr; N A Roseman; Christopher K Mathews; Mary B Slabaugh
Cloning of the vaccinia virus ribonucleotide reductase small subunit gene. Characterization of the gene product expressed in Escherichia coli.
The Journal of biological chemistry 1992;267(3):1705-11.
1991: J Han; E T Adman; T Beppu; Rachel Codd; H C Freeman; L L Huq; Thomas M Loehr; Joann Sanders-Loehr
Resonance Raman spectra of plastocyanin and pseudoazurin: evidence for conserved cysteine ligand conformations in cupredoxins (blue copper proteins).
Biochemistry 1991;30(45):10904-13.
1991: G Backes; V L Davidson; F Huitema; Johannis A Duine; Joann Sanders-Loehr
Characterization of the tryptophan-derived quinone cofactor of methylamine dehydrogenase by resonance Raman spectroscopy.
Biochemistry 1991;30(38):9201-10.
1990: Margareta Sahlin; Britt-Marie Sjöberg; G Backes; Thomas M Loehr; Joann Sanders-Loehr
Activation of the iron-containing B2 protein of ribonucleotide reductase by hydrogen peroxide.
Biochemical and biophysical research communications 1990;167(2):813-8.
1989: G Backes; Margareta Sahlin; Britt-Marie Sjöberg; Thomas M Loehr; Joann Sanders-Loehr
Resonance Raman spectroscopy of ribonucleotide reductase. Evidence for a deprotonated tyrosyl radical and photochemistry of the binuclear iron center.
Biochemistry 1989;28(4):1923-9.
1988: K Zhang; E A Stern; F Ellis; Joann Sanders-Loehr; A K Shiemke
The active site of hemerythrin as determined by X-ray absorption fine structure.
Biochemistry 1988;27(19):7470-9.
1988: K D Sharma; Thomas M Loehr; Joann Sanders-Loehr; M Husain; V L Davidson
Resonance Raman spectroscopy of amicyanin, a blue copper protein from Paracoccus denitrificans.
The Journal of biological chemistry 1988;263(7):3303-6.
1988: Judith Mary Nocek; Donald M Kurtz; J T Sage; Y M Xia; P Debrunner; A K Shiemke; Joann Sanders-Loehr; Thomas M Loehr
Nitric oxide adducts of the binuclear iron site of hemerythrin: spectroscopy and reactivity.
Biochemistry 1988;27(3):1014-24.
1988: Joann Sanders-Loehr
Involvement of oxo-bridged binuclear iron centers in oxygen transport, oxygen reduction, and oxygenation.
Progress in clinical and biological research 1988;274():193-209.
1987: Y Mino; Thomas M Loehr; K Wada; H Matsubara; Joann Sanders-Loehr
Hydrogen bonding of sulfur ligands in blue copper and iron-sulfur proteins: detection by resonance Raman spectroscopy.
Biochemistry 1987;26(25):8059-65.
1987: Britt-Marie Sjöberg; Joann Sanders-Loehr; Thomas M Loehr
Identification of a hydroxide ligand at the iron center of ribonucleotide reductase by resonance Raman spectroscopy.
Biochemistry 1987;26(14):4242-7.
1985: Ronald E Stenkamp; Larry Sieker; L H Jensen; J D McCallum; Joann Sanders-Loehr
Active site structures of deoxyhemerythrin and oxyhemerythrin.
Proceedings of the National Academy of Sciences of the United States of America 1985;82(3):713-6.
1984: G S Lukat; Donald M Kurtz; A K Shiemke; Thomas M Loehr; Joann Sanders-Loehr
Sulfide-bridged derivatives of the binuclear iron site of hemerythrin at both met and semi-met oxidation levels.
Biochemistry 1984;23(26):6416-22.
1984: J D McCallum; A K Shiemke; Joann Sanders-Loehr
Hydroxide ion binding to methemerythrin. An investigation by resonance Raman and difference spectroscopy.
Biochemistry 1984;23(12):2819-25.
1983: W Maret; M Zeppezauer; Joann Sanders-Loehr; Thomas M Loehr
Resonance Raman spectra of copper(II)-substituted liver alcohol dehydrogenase: a type 1 copper analogue.
Biochemistry 1983;22(13):3202-6.
1982: B M Sjöberg; Thomas M Loehr; Joann Sanders-Loehr
Raman spectral evidence for a mu-oxo bridge in the binuclear iron center of ribonucleotide reductase.
Biochemistry 1982;21(1):96-102.