Access the full text.
Sign up today, get DeepDyve free for 14 days.
L. Lad, M. Mewies, J. Basran, N. Scrutton, E. Raven (2002)
Role of histidine 42 in ascorbate peroxidase. Kinetic analysis of the H42A and H42E variants.European journal of biochemistry, 269 13
N. Patel, D. Jones, E. Raven (2000)
Investigation of the haem-nicotinate interaction in leghaemoglobin. Role of hydrogen bonding.European journal of biochemistry, 267 9
Adrian Hill, S. Modi, M. Sutcliffe, D. Turner, D. Gilfoyle, Andrew Smith, B. Tam, E. Lloyd (1997)
Chemical, spectroscopic and structural investigation of the substrate-binding site in ascorbate peroxidase.European journal of biochemistry, 248 2
E. Raven, A. Celik, P. Cullis, R. Sangar, M. Sutcliffe (2001)
Engineering the active site of ascorbate peroxidase.Biochemical Society transactions, 29 Pt 2
P. Montellano (1987)
Control of the catalytic activity of prosthetic heme by the structure of hemoproteinsAccounts of Chemical Research, 20
H. Pappa, W. Patterson, T. Poulos (1996)
The homologous tryptophan critical for cytochrome c peroxidase function is not essential for ascorbate peroxidase activityJBIC Journal of Biological Inorganic Chemistry, 1
W. Patterson, T. Poulos (1994)
Characterization and crystallization of recombinant pea cytosolic ascorbate peroxidase.The Journal of biological chemistry, 269 25
C. Appleby, W. Blumberg, J. Bradbury, W. Fuchsman, J. Peisach, B. Wittenberg, J. Wittenberg, P. Wright (1982)
The Mobile Distal Histidine of Leghemoglobin: Does it Control Oxygen Binding Kinetics?
G. Sievers, P. Gadsby, J. Peterson, Andrew Thomson (1983)
Magnetic circular dichroism spectra of soybean leghaemoglocin a at room temperature and 4.2 KBiochimica et Biophysica Acta, 742
W. Patterson, T. Poulos (1995)
Crystal structure of recombinant pea cytosolic ascorbate peroxidase.Biochemistry, 34 13
D. Groden, E. Beck (1979)
H2O2 destruction by ascorbate-dependent systems from chloroplasts.Biochimica et biophysica acta, 546 3
D. Ollis, C. Appleby, P. Colman, A. Cutten, J. Guss, M. Venkatappa, H. Freeman (1983)
Crystal Structure of Soybean Ferric Leghaemoglobin a Nicotinate at a Resolution of 3.3ǺAustralian Journal of Chemistry, 36
John Dawson (1988)
Probing structure-function relations in heme-containing oxygenases and peroxidases.Science, 240 4851
M. Kvaratskhelia, C. Winkel, R. Thorneley (1997)
Purification and Characterization of a Novel Class III Peroxidase Isoenzyme from Tea Leaves, 114
P. Ellis, C. Appleby, J. Guss, W. Hunter, D. Ollis, H. Freeman (1997)
Structure of ferric soybean leghemoglobin a nicotinate at 2.3 A resolution.Acta crystallographica. Section D, Biological crystallography, 53 Pt 3
M. Davies, C. Mathieu, A. Puppo (1998)
Leghemoglobin: Properties and ReactionsAdvances in Inorganic Chemistry, 46
M. Kvaratskhelia, C. Winkel, M. Naldrett, R. Thorneley (1999)
A Novel High Activity Cationic Ascorbate Peroxidase from Tea (Camellia sinensis) — A Class III Peroxidase with Unusual Substrate SpecificityJournal of Plant Physiology, 154
Deborah Jones, N. Patel, M. Cheesman, A. Thomson, E. Raven (2002)
Leghaemoglobin: a model for the investigation of haem protein axial ligationInorganica Chimica Acta, 331
G. Kelly, E. Latzko (1979)
Soluble ascorbate peroxidaseThe Science of Nature, 66
A. Celik, P. Cullis, E. Raven (2000)
Catalytic oxidation of p-cresol by ascorbate peroxidase.Archives of biochemistry and biophysics, 373 1
D. Mandelman, J. Jamal, T. Poulos (1998)
Identification of two electron-transfer sites in ascorbate peroxidase using chemical modification, enzyme kinetics, and crystallography.Biochemistry, 37 50
D. Jones, R. Badii, F. Rosell, E. Lloyd (1998)
Bacterial expression and spectroscopic characterization of soybean leghaemoglobin a.The Biochemical journal, 330 ( Pt 2)
L. Marquez, Mannix Quitoriano, B. Zilinskas, H. Dunford (1996)
Kinetic and spectral properties of pea cytosolic ascorbate peroxidaseFEBS Letters, 389
E. Bursey, T. Poulos (2000)
Two substrate binding sites in ascorbate peroxidase: the role of arginine 172.Biochemistry, 39 25
Iron protoporphyrin(IX) is one of the most versatile and widespread pieces of catalytic machinery known in biology and is a key component of a multitude of proteins and enzymes. One of most challenging questions in this area has been to identify and understand the relationships that exist between different classes of haem proteins and to use protein engineering methods to rationalize the mechanisms by which the protein structure controls the specific chemical reactivity of the haem group. The application of this approach to the haem enzyme ascorbate peroxidase and the haem protein leghaemoglobin is discussed. © 2002 Wiley Periodicals, Inc. Heteroatom Chem 13:501–505, 2002; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/hc.10094
Heteroatom Chemistry – Wiley
Published: Jan 1, 2002
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.