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PDBsum entry 1h5d
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Oxidoreductase
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PDB id
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1h5d
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The catalytic pathway of horseradish peroxidase at high resolution.
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Authors
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G.I.Berglund,
G.H.Carlsson,
A.T.Smith,
H.Szöke,
A.Henriksen,
J.Hajdu.
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Ref.
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Nature, 2002,
417,
463-468.
[DOI no: ]
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PubMed id
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Abstract
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A molecular description of oxygen and peroxide activation in biological systems
is difficult, because electrons liberated during X-ray data collection reduce
the active centres of redox enzymes catalysing these reactions. Here we describe
an effective strategy to obtain crystal structures for high-valency redox
intermediates and present a three-dimensional movie of the X-ray-driven
catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP).
We also describe separate experiments in which high-resolution structures could
be obtained for all five oxidation states of HRP, showing such structures with
preserved redox states for the first time.
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Figure 1.
Figure 1: The five oxidation states of horseradish peroxidase.
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Figure 4.
Figure 4: Spectra and refined high-resolution structures for the
five oxidation states of horseradish peroxidase. Accession
codes are shown. The structures were captured at high
concentrations in individual experiments (Methods) and were
obtained from the first few degrees of data (Table 2 of the
Supplementary Information). a, Ferric enzyme. b, Ferrous enzyme.
c, Compound III (Fe -O bond distance, 1.8 Å). d, Compound I (Fe
-O bond distance, 1.7 Å). e, Compound II (Fe -O bond distance,
1.8 Å). SigmaA-weighted^30 2mF[obs] -DF[calc] maps contoured at
1  .
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2002,
417,
463-468)
copyright 2002.
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Secondary reference #1
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Title
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The structures of the horseradish peroxidase c-Ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates.
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Authors
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A.Henriksen,
A.T.Smith,
M.Gajhede.
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Ref.
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J Biol Chem, 1999,
274,
35005-35011.
[DOI no: ]
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PubMed id
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Figure 2.
Fig. 2. A, the 1.5  simulated
anneal omit 2 F[o]  F[c]
density surrounding the cyanide and the water molecule in the
active site of the HRPC-CN-FA complex and the 0.3 simulated
anneal omit 2 F[o] F[c]
density surrounding FA molecules in the HRPC-CN-FA complex. B,
the active site of HRPC-CN-FA. Hydrogen bonds between active
site residues and ligands are indicated with dotted black lines.
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Figure 3.
Fig. 3. Proposed mechanism for substrate oxidation in
plant peroxidases. First, the active site arginine (Arg38 in
HRPC) donates a hydrogen bond to the phenolic oxygen of the
reducing substrate. This hydrogen bond will assist proton
transfer from the phenolic oxygen to active site histidine (His
42 in HRPC) through an active site water molecule held in
position by the backbone oxygen of a conserved proline residue
(Pro139 in HRPC). The electron is transferred to the heme group
via the C-18 methyl-C-20 heme edge. Then compound II reduction
is assisted by similar a proton transfer. The proton can be
transferred to the ferryl oxygen through the active site water
molecule situated equidistant between the distal histidine and
the expected position of the ferryl oxygen of compound II,
regenerating the resting state enzyme and a water molecule.
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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Secondary reference #2
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Title
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Crystal structure of horseradish peroxidase c at 2.15 a resolution.
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Authors
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M.Gajhede,
D.J.Schuller,
A.Henriksen,
A.T.Smith,
T.L.Poulos.
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Ref.
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Nat Struct Biol, 1997,
4,
1032-1038.
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PubMed id
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Secondary reference #3
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Title
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Expression of a synthetic gene for horseradish peroxidase c in escherichia coli and folding and activation of the recombinant enzyme with ca2+ and heme.
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Authors
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A.T.Smith,
N.Santama,
S.Dacey,
M.Edwards,
R.C.Bray,
R.N.Thorneley,
J.F.Burke.
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Ref.
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J Biol Chem, 1990,
265,
13335-13343.
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PubMed id
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