Sökning: onr:"swepub:oai:DiVA.org:umu-18882" >
Optical spectra of ...
Optical spectra of lactoperoxidase as a function of solvent
-
- Zelent, B (författare)
- University of Pennsylvania
-
- Yano, T (författare)
- University of Pennsylvania
-
- Ohlsson, P-I (författare)
- Umeå universitet,Institutionen för fysiologisk botanik,Umeå Plant Science Centre (UPSC)
-
visa fler...
-
- Smith, ML (författare)
- Anabolic Laboratories, Inc., Tempe, AZ
-
- Paul, Jan (författare)
- Luleå tekniska universitet,Materialvetenskap
-
- Vanderkooi, JM (författare)
- University of Pennsylvania
-
visa färre...
-
(creator_code:org_t)
- 2005-11-08
- 2005
- Engelska.
-
Ingår i: Biochemistry. - Washington : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 44:48, s. 15953-15959
- Relaterad länk:
-
https://urn.kb.se/re...
-
visa fler...
-
https://doi.org/10.1...
-
https://urn.kb.se/re...
-
visa färre...
Abstract
Ämnesord
Stäng
- The iron of lactoperoxidase is predominantly high-spin at ambient temperature. Optical spectra of lactoperoxidase indicate that the iron changes from high-spin to low-spin in the temperature range from room temperature to 20 K. The transformation is independent of whether the enzyme is in glycerol/water or solid sugar glass. Addition of the inhibitor benzohydroxamic acid increases the amount of the low-spin form, and again the transformation is independent of whether the protein is in an aqueous solution or a nearly anhydrous sugar. In contrast to lactoperoxidase, horseradish peroxidase remains high-spin over the temperature excursion in both solvents and with addition of benzohydroxamic acid. We conclude that details of the heme pocket of lactoperoxidase allow ligation changes with temperature that are dependent upon the apoprotein but independent of solvent fluctuations. At low pH, lactoperoxidase shows a solvent-dependent transition; the high-spin form is predominant in anhydrous sugar glass, but in the presence of water, the low-spin form is also present in abundance. The active site of lactoperoxidase is not as tightly constrained at low pH as at neutrality, though the enzyme is active over a wide pH range.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Fysik -- Annan fysik (hsv//swe)
- NATURAL SCIENCES -- Physical Sciences -- Other Physics Topics (hsv//eng)
Nyckelord
- molecular-dynamics simulations
- infrared spectroscopy
- absorption-spectroscopy
- prosthetic group
- resonance raman
- heme-proteins
- active site
- peroxidase
- myeloperoxidase
- binding
- Fysik
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas