Fine Sampling of the R→T Quaternary‐Structure Transition of a Tetrameric Hemoglobin. Issue 3 (7th December 2016)

• Record Type: Journal Article
• Authors: Vitagliano, Luigi; Mazzarella, Lelio; Merlino, Antonello; Vergara, Alessandro
• Is Part Of: Chemistry. Volume 23:Issue 3(2017)
• Page Start: 605
• Page End: 613
• Publication Date: 2016-12-07
• Subjects: allosterism -- IR spectroscopy -- metalloproteins -- protein structures -- X-ray diffraction; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201603421
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract: Although the end points of the functional transitions of tetrameric hemoglobins (Hbs) have been well characterized, atomic‐resolution data on R–T intermediate states are extremely limited. Herein, the X‐ray structures of two independent tetramers of the fully ligated carbomonoxy form of Trematomus newnesi hemoglobin (Hb1Tn) within the same crystal are described. These structures show peculiar features in the heme pocket, EF corner, and tertiary/quaternary structure. Distal histidine side chains have a propensity to swing out of the heme pocket and thus allow compression of the EF corner. In this rotameric state, the distal His group does not interact with the CO ligand, consistent with FTIR spectra recorded in solution. At the quaternary‐structure level, one tetramer is an intermediate R–T state, whereas the other assumes a T‐like structure. Altogether, the structures of these tetramers provide the best available atomic‐level picture of the R→T transition of vertebrate Hbs. Abstract : Spot the difference : The structures of two Antarctic fish tetrameric hemoglobins provided a detailed atomic‐level picture of the R→T transition. They show peculiar features in the heme pocket, EF corner and tertiary/quaternary structure. Their positions on the R–T transition pathway were elucidated inter alia by means of difference distance matrices (see figure).