German biochemist and Nobel laureate (born 1937)
Robert Huber
(
German pronunciation:
[??oːb??t
?huːb?]
ⓘ
; born 20 February 1937) is a German
biochemist
and
Nobel laureate
.
[6]
[7]
[8]
[9]
[10]
known for his work crystallizing an intra
membrane protein
important in
photosynthesis
and subsequently applying X-ray crystallography to elucidate the protein's structure.
Education and early life
[
edit
]
He was born on 20 February 1937 in
Munich
where his father, Sebastian, was a bank cashier. He was educated at the Humanistisches Karls-Gymnasium from 1947 to 1956 and then studied
chemistry
at the
Technische Hochschule
, receiving his diploma in 1960. He stayed, and did research into using
crystallography
to elucidate the structure of
organic compounds
.
Career
[
edit
]
In 1971 he became a director at the
Max Planck Institute for Biochemistry
where his team developed methods for the crystallography of
proteins
.
In 1988 he received the
Nobel Prize for Chemistry
jointly with
Johann Deisenhofer
and
Hartmut Michel
. The trio were recognized for their work in first crystallizing an intramembrane protein important in photosynthesis in
purple bacteria
, and subsequently applying X-ray crystallography to elucidate the protein's structure.
[11]
The information provided the first insight into the structural bodies that performed the integral function of photosynthesis. This insight could be translated to understand the more complex analogue of photosynthesis in
cyanobacteria
[12]
which is essentially the same as that in
chloroplasts
of higher plants.
[
citation needed
]
In 2006, he took up a post at the
Cardiff University
to spearhead the development of Structural Biology at the university on a part-time basis.
[13]
Since 2005 he has been doing research at the
Center for medical biotechnology
of the
University of Duisburg-Essen
.
Huber was one of the original editors of the
Encyclopedia of Analytical Chemistry
.
Awards and honours
[
edit
]
In 1977 Huber was awarded the
Otto Warburg Medal
.
[14]
In 1988 he was awarded the Nobel Prize and in 1992 the
Sir Hans Krebs Medal
.
[15]
Huber was elected a member of
Pour le Merite for Sciences and Arts
, in 1993
[16]
and
Foreign Member of the Royal Society (ForMemRS) in 1999
.
[2]
His certificate of election reads:
Huber has built up, led and still leads the most productive protein crystallography laboratory in Europe. His own contributions to crystallography, made over a period of some 25 years, are prodigious. For his PhD thesis he solved the chemical formula of the important insect hormone edtyson which had eluded the chemists. He then demonstrated that the tertiary fold of the polypeptide chain in the haemoglobin of the fly
larva
chironomus
closely resembled that in Kendrew's sperm whale
myoglobin
, indicating for the first time that this fold had been preserved throughout evolution.
Huber's next achievement was the solution of the structure of
trypsin inhibitor
and the demonstration that in its complex with trypsin it mimicked the tetrahedral transition state of the enzyme's substrate. Since then he has determined the structures of many other proteinases, their inactive precursors and their inhibitors, and has established himself as the world authority in this field. Outstanding structures are those of
procarboxypeptidase
, which led to the discovery of the remarkable activation mechanism of this enzyme, and of the complex of
thrombin
with
hirudin
, which showed the molecular mechanism of inhibition of blood clotting by this leech toxin.
In parallel with this work, Huber solved the structures of several
immunoglobulin
fragments. He was the first to determine the structure of the complement-activating F-fragment, which was also the first variable and the first constant domains in Fab-fragments.
Huber's structure of
citrate synthase
revealed a striking example of a conformational change undergone by an enzyme on combination with its substrate by a process of induced fit.
Huber shared the Nobel Prize for Chemistry in 1988 with Michel and Deisenhofer for their determination of the remarkable and supremely important structures of the photochemical reaction centre of Rhodopseudomonas viridis and of
phycocyanin
, the light harvesting protein of the
blue-green alga
Mastiglocadus laminosus. This protein binds linear
tetrapyrroles
in a
tertiary fold
reminiscent of the
globins
, which brought Huber back full circle to his first structure,
erythrocruerin
,
Huber has also determined the structures of several copper-containing
electron-transfer proteins
, including that of
ascorbate oxidase
, and of other metallo-enzymes. These studies have thrown new light on electron-transfer systems and on zinc coordination in proteins. He has also solved the structure of an important class of calcium binding proteins ? the annexins. Finally his very accurate structures have provided important insights into the different degrees of mobility within protein molecules.
Huber has published some 400 papers.
[1]
Personal life
[
edit
]
Huber is married and has four children.
[
citation needed
]
References
[
edit
]
- ^
a
b
"Certificate of election EC/1999/43: Huber, Robert"
. London:
Royal Society
. Archived from
the original
on 2019-07-08.
- ^
a
b
"Professor Robert Huber ForMemRS"
. London:
Royal Society
. Archived from
the original
on 2015-10-26.
- ^
Huber, R; Deisenhofer, J; Colman, P. M.; Matsushima, M; Palm, W (1976). "Crystallographic structure studies of an IgG molecule and an Fc fragment".
Nature
.
264
(5585): 415?20.
Bibcode
:
1976Natur.264..415H
.
doi
:
10.1038/264415a0
.
PMID
1004567
.
S2CID
4193312
.
- ^
Huber, R; Deisenhofer, J; Colman, P. M.; Epp, O; Fehlhammer, H; Palm, W (1976). "Proceedings: X-ray diffraction analysis of immunoglobulin structure".
Hoppe-Seyler's Zeitschrift fur physiologische Chemie
.
357
(5): 614?5.
PMID
964922
.
- ^
Colman, P. M.
;
Deisenhofer, J
;
Huber, R
(1976). "Structure of the human antibody molecule Kol (immunoglobulin G1): An electron density map at 5 a resolution".
Journal of Molecular Biology
.
100
(3): 257?78.
doi
:
10.1016/s0022-2836(76)80062-9
.
PMID
1255713
.
- ^
Engh, R. A.; Huber, R. (1991). "Accurate bond and angle parameters for X-ray protein structure refinement".
Acta Crystallographica Section A
.
47
(4): 392?400.
doi
:
10.1107/S0108767391001071
.
- ^
Groll, M; Ditzel, L; Lowe, J; Stock, D; Bochtler, M; Bartunik, H. D.; Huber, R (1997). "Structure of 20S proteasome from yeast at 2.4 a resolution".
Nature
.
386
(6624): 463?71.
Bibcode
:
1997Natur.386..463G
.
doi
:
10.1038/386463a0
.
PMID
9087403
.
S2CID
4261663
.
- ^
Deisenhofer, J.; Epp, O.; Miki, K.; Huber, R.; Michel, H. (1984). "X-ray structure analysis of a membrane protein complex".
Journal of Molecular Biology
.
180
(2): 385?398.
doi
:
10.1016/S0022-2836(84)80011-X
.
PMID
6392571
.
- ^
Robert Huber autobiographical information at www.nobel.org
- ^
Huber, R.; Swanson, R. V.; Deckert, G.; Warren, P. V.; Gaasterland, T.; Young, W. G.; Lenox, A. L.; Graham, D. E.; Overbeek, R.; Snead, M. A.; Keller, M.; Aujay, M.; Feldman, R. A.; Short, J. M.; Olsen, G. J. (1998).
"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus"
.
Nature
.
392
(6674): 353?8.
Bibcode
:
1998Natur.392..353D
.
doi
:
10.1038/32831
.
PMID
9537320
.
- ^
Deisenhofer, J.
; Epp, O.; Miki, K.;
Huber, R.
;
Michel, H.
(1985). "Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3A resolution".
Nature
.
318
(6047): 618?624.
Bibcode
:
1985Natur.318..618D
.
doi
:
10.1038/318618a0
.
PMID
22439175
.
S2CID
1551692
.
- ^
Guskov, A.; Kern, J.; Gabdulkhakov, A.; Broser, M.; Zouni, A.; Saenger, W. (2009). "Cyanobacterial photosystem II at 2.9-A resolution and the role of quinones, lipids, channels and chloride".
Nature Structural & Molecular Biology
.
16
(3): 334?42.
doi
:
10.1038/nsmb.1559
.
PMID
19219048
.
S2CID
23034289
.
- ^
Smith, Alexandra (2006-10-24).
"Nobel chemist joins Cardiff University"
.
The Guardian
. Retrieved
14 September
2015
.
- ^
"Otto-Warburg-Medal"
. GBM
. Retrieved
12 January
2014
.
- ^
"Superstars of Science"
. Retrieved
12 January
2015
.
- ^
"Curriculum vitae"
. Max Planck Institute
. Retrieved
11 January
2015
.
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