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2.
Heart Lung ; 50(5): 579-586, 2021.
Article in English | MEDLINE | ID: mdl-34077826

ABSTRACT

BACKGROUND: Recent interest in the 'weekend effect' has been expanded to cardiovascular intensive care units, yet the impact of off-hours admission on mortality and cardiovascular ICU (CICU) length of stay remains uncertain. OBJECTIVES: We examine the association between CICU admission day and time with mortality. Additionally, length-of-stay was also evaluated in relation to admission time. METHODS: A single-center, retrospective cohort study was conducted including 10,638 adult patients admitted to a CICU in a tertiary-care academic medical center from July 1, 2012 to June 30, 2019. ICU mortality and length-of-stay were assessed by admission day and time adjusting for comorbid conditions and other clinical variables. We used logistic regression models to evaluate the factors associated with mortality and a generalized linear model (GLM) with log link function and gamma distribution was used to evaluate the factors associated with ICU length of stay. RESULTS: Compared to weekday-day admissions, we observed an increased mortality for weekend-day for all admissions (6.5 vs 9.6%, Adjusted OR: 1.32 (1.03-1.72)), and for medical CICU admissions (7.6 vs 9.9%, Adjusted OR: 1.35 (1.02-1.79)). Additionally, compared to weekday-day, weekday-night admission was associated with 7% longer ICU length of stay in surgical ICU patients, 7% shorter length of stay in medical ICU patients. CONCLUSION: Admission to this open-model CICU during weekend hours (Saturday 08:00-Sunday 17:59) versus nights or weekdays is associated with increased mortality. ICU staffing care models should not significantly change based on the day of the week.


Subject(s)
Hospitalization , Intensive Care Units , Adult , Hospital Mortality , Humans , Retrospective Studies , Time Factors
3.
J Am Chem Soc ; 138(49): 16016-16023, 2016 12 14.
Article in English | MEDLINE | ID: mdl-27960340

ABSTRACT

We report on the protonation state of Helicobacter pylori catalase compound II. UV/visible, Mössbauer, and X-ray absorption spectroscopies have been used to examine the intermediate from pH 5 to 14. We have determined that HPC-II exists in an iron(IV) hydroxide state up to pH 11. Above this pH, the iron(IV) hydroxide complex transitions to a new species (pKa = 13.1) with Mössbauer parameters that are indicative of an iron(IV)-oxo intermediate. Recently, we discussed a role for an elevated compound II pKa in diminishing the compound I reduction potential. This has the effect of shifting the thermodynamic landscape toward the two-electron chemistry that is critical for catalase function. In catalase, a diminished potential would increase the selectivity for peroxide disproportionation over off-pathway one-electron chemistry, reducing the buildup of the inactive compound II state and reducing the need for energetically expensive electron donor molecules.


Subject(s)
Catalase/chemistry , Helicobacter pylori/enzymology , Hydroxides/chemistry , Iron Compounds/chemistry , Binding Sites , Catalase/metabolism , Hydrogen-Ion Concentration , Hydroxides/metabolism , Iron Compounds/metabolism , Molecular Structure , Spectrophotometry, Ultraviolet , Spectroscopy, Mossbauer , X-Ray Absorption Spectroscopy
4.
J Am Chem Soc ; 136(25): 9124-31, 2014 Jun 25.
Article in English | MEDLINE | ID: mdl-24875119

ABSTRACT

To provide insight into the iron(IV)hydroxide pK(a) of histidine ligated heme proteins, we have probed the active site of myoglobin compound II over the pH range of 3.9-9.5, using EXAFS, Mössbauer, and resonance Raman spectroscopies. We find no indication of ferryl protonation over this pH range, allowing us to set an upper limit of 2.7 on the iron(IV)hydroxide pK(a) in myoglobin. Together with the recent determination of an iron(IV)hydroxide pK(a) ∼ 12 in the thiolate-ligated heme enzyme cytochrome P450, this result provides insight into Nature's ability to tune catalytic function through its choice of axial ligand.


Subject(s)
Histidine/chemistry , Hydroxides/chemistry , Iron/chemistry , Myoglobin/chemistry , Catalysis , Catalytic Domain , Hydrogen-Ion Concentration , Ligands , Molecular Structure , Spectroscopy, Mossbauer , Spectrum Analysis, Raman , X-Ray Absorption Spectroscopy
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