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PDBsum entry 1gdi
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Oxygen transport
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PDB id
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1gdi
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Contents |
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* Residue conservation analysis
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J Mol Biol
264:152-161
(1996)
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PubMed id:
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The binding of carbon monoxide and nitric oxide to leghaemoglobin in comparison with other haemoglobins.
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E.H.Harutyunyan,
T.N.Safonova,
I.P.Kuranova,
A.N.Popov,
A.V.Teplyakov,
G.V.Obmolova,
B.K.Valnshtein,
G.G.Dodson,
J.C.Wilson.
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ABSTRACT
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Haemoglobins have the ability to discriminate between oxygen and other diatomic
molecules. To further understanding of this process the X-ray crystal structures
of carbonmonoxy and nitrosyl-leghaemoglobin have been determined at 1.8 A
resolution. The ligand geometry is discussed in detail and the controversial
issue of bent versus linear carbon monoxide binding is addressed. The bond angle
of 160 degrees for CO-leghaemoglobin is in conflict with recent spectroscopy
results on myoglobin but is consistent with angles obtained for myoglobin X-ray
crystal structures. In contrast to the numerous carbon monoxide studies, very
little stereochemical information is available for the nitric oxide adduct of
haemoglobin. This is provided by the X-ray structure of NO-leghaemoglobin, which
conforms to expected geometry with an Fe-NO angle of 147 degrees and a
lengthened iron-proximal histidine bond. Thus crystallographic evidence is given
for the predicted weakening of this bond on the binding of nitric oxide.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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L.Sael,
D.La,
B.Li,
R.Rustamov,
and
D.Kihara
(2008).
Rapid comparison of properties on protein surface.
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Proteins,
73,
1.
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E.Baudouin,
L.Pieuchot,
G.Engler,
N.Pauly,
and
A.Puppo
(2006).
Nitric oxide is formed in Medicago truncatula-Sinorhizobium meliloti functional nodules.
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Mol Plant Microbe Interact,
19,
970-975.
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A.Karlsson,
J.V.Parales,
R.E.Parales,
D.T.Gibson,
H.Eklund,
and
S.Ramaswamy
(2005).
NO binding to naphthalene dioxygenase.
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J Biol Inorg Chem,
10,
483-489.
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PDB codes:
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D.Pozzi,
G.Amiconi,
A.Arcovito,
M.Girasole,
and
A.C.Castellano
(2005).
Haem conformation of amphibian nytrosylhaemoglobins detected by XANES spectroscopy.
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Eur Phys J E Soft Matter,
16,
373-379.
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S.Galijasevic,
G.M.Saed,
M.P.Diamond,
and
H.M.Abu-Soud
(2004).
High dissociation rate constant of ferrous-dioxy complex linked to the catalase-like activity in lactoperoxidase.
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J Biol Chem,
279,
39465-39470.
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D.M.Copeland,
A.H.West,
and
G.B.Richter-Addo
(2003).
Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane.
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Proteins,
53,
182-192.
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PDB codes:
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J.Friedman,
L.Lad,
R.Deshmukh,
H.Li,
A.Wilks,
and
T.L.Poulos
(2003).
Crystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis. Implications for O2 activation.
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J Biol Chem,
278,
34654-34659.
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PDB codes:
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S.Nagatomo,
M.Nagai,
N.Shibayama,
and
T.Kitagawa
(2002).
Differences in changes of the alpha1-beta2 subunit contacts between ligand binding to the alpha and beta subunits of hemoglobin A: UV resonance raman analysis using Ni-Fe hybrid hemoglobin.
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Biochemistry,
41,
10010-10020.
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J.T.Trent,
A.N.Hvitved,
and
M.S.Hargrove
(2001).
A model for ligand binding to hexacoordinate hemoglobins.
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Biochemistry,
40,
6155-6163.
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C.Jung
(2000).
Insight into protein structure and protein-ligand recognition by Fourier transform infrared spectroscopy.
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J Mol Recognit,
13,
325-351.
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D.M.Lawson,
C.E.Stevenson,
C.R.Andrew,
and
R.R.Eady
(2000).
Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclase.
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EMBO J,
19,
5661-5671.
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PDB codes:
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H.M.Abu-Soud,
and
S.L.Hazen
(2000).
Nitric oxide modulates the catalytic activity of myeloperoxidase.
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J Biol Chem,
275,
5425-5430.
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H.Shimizu,
E.Obayashi,
Y.Gomi,
H.Arakawa,
S.Y.Park,
H.Nakamura,
S.Adachi,
H.Shoun,
and
Y.Shiro
(2000).
Proton delivery in NO reduction by fungal nitric-oxide reductase. Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes.
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J Biol Chem,
275,
4816-4826.
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PDB codes:
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M.S.Hargrove,
E.A.Brucker,
B.Stec,
G.Sarath,
R.Arredondo-Peter,
R.V.Klucas,
J.S.Olson,
and
G.N.Phillips
(2000).
Crystal structure of a nonsymbiotic plant hemoglobin.
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Structure,
8,
1005-1014.
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PDB code:
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A.M.Rich,
P.J.Ellis,
L.Tennant,
P.E.Wright,
R.S.Armstrong,
and
P.A.Lay
(1999).
Determination of Fe-ligand bond lengths and the Fe-N-O bond angles in soybean ferrous and ferric nitrosylleghemoglobin a using multiple-scattering XAFS analyses.
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Biochemistry,
38,
16491-16499.
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C.Mathieu,
S.Moreau,
P.Frendo,
A.Puppo,
and
M.J.Davies
(1998).
Direct detection of radicals in intact soybean nodules: presence of nitric oxide-leghemoglobin complexes.
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Free Radic Biol Med,
24,
1242-1249.
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D.Nurizzo,
F.Cutruzzolà,
M.Arese,
D.Bourgeois,
M.Brunori,
C.Cambillau,
and
M.Tegoni
(1998).
Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosa.
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Biochemistry,
37,
13987-13996.
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PDB codes:
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N.L.Chan,
P.H.Rogers,
and
A.Arnone
(1998).
Crystal structure of the S-nitroso form of liganded human hemoglobin.
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Biochemistry,
37,
16459-16464.
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PDB code:
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S.Nagashima,
M.Nakasako,
N.Dohmae,
M.Tsujimura,
K.Takio,
M.Odaka,
M.Yohda,
N.Kamiya,
and
I.Endo
(1998).
Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms.
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Nat Struct Biol,
5,
347-351.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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